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Torbjörn Drakenberg - One of the best experts on this subject based on the ideXlab platform.

  • Interaction of bovine Coagulation Factor X and its glutamic-acid-containing fragments with phospholipid membranes. A surface plasmon resonance study.
    European journal of biochemistry, 2002
    Co-Authors: Eva-maria Erb, Johan Stenflo, Torbjörn Drakenberg
    Abstract:

    The interaction of blood Coagulation Factor X and its Gla-containing fragments with negatively charged phospholipid membranes composed of 25 mol% phosphatidylserine (PtdSer) and 75 mol% phosphatidylcholine (PtdCho) was studied by surface plasmon resonance. The binding to 100 mol% PtdCho membranes was negligible. The calcium dependence in the membrane binding was evaluated for intact bovine Factor X (Factor X) and the fragment containing the Gla-domain and the N-terminal EGF (epidermal growth Factor)-like domain, Gla-EGFN, from Factor X. Both proteins show the same calcium dependence in the membrane binding. Calcium binding is cooperative and half-maXimum binding was observed at 1.5 mm and 1.4 mm, with the best fit to the eXperimental data with three cooperatively bound calcium ions for both the intact protein and the fragment. The dissociation constant (Kd) for binding to membranes containing 25 mol% PtdSer decreased from 4.6 microm for the isolated Gla-domain to 1 microm for the fragments Gla-EGFN and Gla-EGFNC (the Gla-domain and both EGF-like domains) fragments and to 40 nm for the entire protein as zymogen, activated enzyme or in the active-site inhibited form. Analysis of the kinetics of adsorption and desorption confirmed the equilibrium binding data.

  • the relative orientation of gla and egf domains in Coagulation Factor X is altered by ca2 binding to the first egf domain a combined nmr small angle X ray scattering study
    Biochemistry, 1996
    Co-Authors: Maria Sunnerhagen, Johan Stenflo, Torbjörn Drakenberg, G A Olah, Sture Forsen, Jill Trewhella
    Abstract:

    Coagulation Factor X is a serine protease containing three noncatalytic domains:  an N-terminal γ-carboXyglutamic acid (Gla)1 domain followed by two epidermal growth Factor (EGF)-like domains. The isolated N-terminal EGF domain binds Ca2+ with a Kd of 10-3 M. When linked to the Gla domain, however, its Ca2+ affinity is increased 10-fold. In this paper, we present the NMR solution structure of the Factor X Gla−EGF domain pair with Ca2+ bound to the EGF domain, as well as small angle X-ray scattering (SAXS) data on the Gla−EGF domain pair with and without Ca2+. Our results show that Ca2+ binding to the EGF domain makes the Gla and EGF domains fold toward each other using the Ca2+ site as a hinge. Presumably, a similar mechanism may be responsible for alterations in the relative orientation of protein domains in many other eXtracellular proteins containing EGF domains with the consensus for Ca2+ binding. The results of the NMR and SAXS measurements reported in this paper confirm our previous result that the ...

  • The relative orientation of Gla and EGF domains in Coagulation Factor X is altered by Ca2+ binding to the first EGF domain. A combined NMR-small angle X-ray scattering study.
    Biochemistry, 1996
    Co-Authors: Maria Sunnerhagen, Johan Stenflo, Torbjörn Drakenberg, G A Olah, Sture Forsen, Jill Trewhella
    Abstract:

    Coagulation Factor X is a serine protease containing three noncatalytic domains: an N-terminal gamma-carboXyglutamic acid (Gla)1 domain followed by two epidermal growth Factor (EGF)-like domains. The isolated N-terminal EGF domain binds Ca2+ with a Kd of 10(-3) M. When linked to the Gla domain, however, its Ca2+ affinity is increased 10-fold. In this paper, we present the NMR solution structure of the Factor X Gla-EGF domain pair with Ca2+ bound to the EGF domain, as well as small angle X-ray scattering (SAXS) data on the Gla-EGF domain pair with and without Ca2+. Our results show that Ca2+ binding to the EGF domain makes the Gla and EGF domains fold toward each other using the Ca2+ site as a hinge. Presumably, a similar mechanism may be responsible for alterations in the relative orientation of protein domains in many other eXtracellular proteins containing EGF domains with the consensus for Ca2+ binding. The results of the NMR and SAXS measurements reported in this paper confirm our previous result that the Gla domain is folded also in its apo state when linked to the EGF domain [Sunnerhagen, M., et al. (1995) Nat. Struct. Biol. 2, 504-509]. Finally, our study clearly demonstrates the powerful combination of NMR and SAXS in the study of modular proteins, since this enables reliable evaluation of both short-range (NMR) and long-range interactions (SAXS).

  • How an epidermal growth Factor (EGF)-like domain binds calcium. High resolution NMR structure of the calcium form of the NH2-terminal EGF-like domain in Coagulation Factor X.
    The Journal of biological chemistry, 1992
    Co-Authors: Maria Selander-sunnerhagen, Egon Persson, Johan Stenflo, Magnus Ullner, Olle Teleman, Torbjörn Drakenberg
    Abstract:

    Domains homologous to the epidermal growth Factor (EGF) are important building blocks for eXtracellular proteins. Proteins containing these domains have been shown to function in such diverse biological processes as blood Coagulation, complement activation, and the developmental determination of embryonic cell fates. Many of these proteins require calcium for their biological function. In the case of Coagulation Factors IX and X and anticoagulants proteins C and S, calcium has been found to bind to the EGF-like domains. We have now determined the three-dimensional structure of the calcium-bound form of the NH2-terminal EGF-like domain in Coagulation Factor X by two-dimensional NMR and simulated folding. Ligands to the calcium ion are the two backbone carbonyls in Gly-47 and Gly-64, as well as the side chains in Gln-49, erythro-beta-hydroXyaspartic acid (Hya) 63, and possibly Asp-46. The conserved Asp-48 is not a ligand in our present structures. The remaining ligands are assumed to be solvent molecules or, in the intact protein, ligands from neighboring domains. Other proteins interacting in a calcium-dependent manner may also contribute ligands. A comparison with the calcium-free form shows that calcium binding induces strictly local structural changes in the domain. Residues corresponding to the side chain ligands in Factor X are conserved in many other proteins, such as the integral membrane protein TAN-1 of human lymphocytes and its developmentally important homolog, Notch, in Drosophila. Calcium binding to EGF-like domains may be crucial for numerous protein-protein interactions involving EGF-like domains in Coagulation Factors, plasma proteins, and membrane proteins. Therefore, there is reason to believe that this novel calcium site plays an important role in the biochemistry of eXtracellular proteins.

  • Three-dimensional structure of the apo form of the N-terminal EGF-like module of blood Coagulation Factor X as determined by NMR spectroscopy and simulated folding.
    Biochemistry, 1992
    Co-Authors: Magnus Ullner, Egon Persson, Johan Stenflo, Torbjörn Drakenberg, Maria Selander, Olle Teleman
    Abstract:

    The three-dimensional structure of a 42-residue fragment containing the N-terminal EGF-like module of blood Coagulation Factor X was determined by means of 2D NMR spectroscopy and computer simulation. The spectroscopic data consisted of 370 NOE distances and 27 dihedral angle constraints. These were used to generate peptide conformations by molecular dynamics simulation. The simulations used a novel functional form for the constraint potentials and were performed with two time steps to ensure rapid eXecution. Apart from preliminary runs to aid assignment of NOEs, 60 runs resulted in 13 accepted structures, which have two antiparallel beta sheets, no alpha helices, and five tight turns. There is no hydrophobic cluster. The root mean square deviation for the backbone of the 13 conformations is 0.65 +/- 0.11 A against their mean conformation. About half of the side chains have well-defined structure. The overall conformation is similar to that of murine EGF.

Johan Stenflo - One of the best experts on this subject based on the ideXlab platform.

  • Interaction of bovine Coagulation Factor X and its glutamic-acid-containing fragments with phospholipid membranes. A surface plasmon resonance study.
    European journal of biochemistry, 2002
    Co-Authors: Eva-maria Erb, Johan Stenflo, Torbjörn Drakenberg
    Abstract:

    The interaction of blood Coagulation Factor X and its Gla-containing fragments with negatively charged phospholipid membranes composed of 25 mol% phosphatidylserine (PtdSer) and 75 mol% phosphatidylcholine (PtdCho) was studied by surface plasmon resonance. The binding to 100 mol% PtdCho membranes was negligible. The calcium dependence in the membrane binding was evaluated for intact bovine Factor X (Factor X) and the fragment containing the Gla-domain and the N-terminal EGF (epidermal growth Factor)-like domain, Gla-EGFN, from Factor X. Both proteins show the same calcium dependence in the membrane binding. Calcium binding is cooperative and half-maXimum binding was observed at 1.5 mm and 1.4 mm, with the best fit to the eXperimental data with three cooperatively bound calcium ions for both the intact protein and the fragment. The dissociation constant (Kd) for binding to membranes containing 25 mol% PtdSer decreased from 4.6 microm for the isolated Gla-domain to 1 microm for the fragments Gla-EGFN and Gla-EGFNC (the Gla-domain and both EGF-like domains) fragments and to 40 nm for the entire protein as zymogen, activated enzyme or in the active-site inhibited form. Analysis of the kinetics of adsorption and desorption confirmed the equilibrium binding data.

  • the relative orientation of gla and egf domains in Coagulation Factor X is altered by ca2 binding to the first egf domain a combined nmr small angle X ray scattering study
    Biochemistry, 1996
    Co-Authors: Maria Sunnerhagen, Johan Stenflo, Torbjörn Drakenberg, G A Olah, Sture Forsen, Jill Trewhella
    Abstract:

    Coagulation Factor X is a serine protease containing three noncatalytic domains:  an N-terminal γ-carboXyglutamic acid (Gla)1 domain followed by two epidermal growth Factor (EGF)-like domains. The isolated N-terminal EGF domain binds Ca2+ with a Kd of 10-3 M. When linked to the Gla domain, however, its Ca2+ affinity is increased 10-fold. In this paper, we present the NMR solution structure of the Factor X Gla−EGF domain pair with Ca2+ bound to the EGF domain, as well as small angle X-ray scattering (SAXS) data on the Gla−EGF domain pair with and without Ca2+. Our results show that Ca2+ binding to the EGF domain makes the Gla and EGF domains fold toward each other using the Ca2+ site as a hinge. Presumably, a similar mechanism may be responsible for alterations in the relative orientation of protein domains in many other eXtracellular proteins containing EGF domains with the consensus for Ca2+ binding. The results of the NMR and SAXS measurements reported in this paper confirm our previous result that the ...

  • The relative orientation of Gla and EGF domains in Coagulation Factor X is altered by Ca2+ binding to the first EGF domain. A combined NMR-small angle X-ray scattering study.
    Biochemistry, 1996
    Co-Authors: Maria Sunnerhagen, Johan Stenflo, Torbjörn Drakenberg, G A Olah, Sture Forsen, Jill Trewhella
    Abstract:

    Coagulation Factor X is a serine protease containing three noncatalytic domains: an N-terminal gamma-carboXyglutamic acid (Gla)1 domain followed by two epidermal growth Factor (EGF)-like domains. The isolated N-terminal EGF domain binds Ca2+ with a Kd of 10(-3) M. When linked to the Gla domain, however, its Ca2+ affinity is increased 10-fold. In this paper, we present the NMR solution structure of the Factor X Gla-EGF domain pair with Ca2+ bound to the EGF domain, as well as small angle X-ray scattering (SAXS) data on the Gla-EGF domain pair with and without Ca2+. Our results show that Ca2+ binding to the EGF domain makes the Gla and EGF domains fold toward each other using the Ca2+ site as a hinge. Presumably, a similar mechanism may be responsible for alterations in the relative orientation of protein domains in many other eXtracellular proteins containing EGF domains with the consensus for Ca2+ binding. The results of the NMR and SAXS measurements reported in this paper confirm our previous result that the Gla domain is folded also in its apo state when linked to the EGF domain [Sunnerhagen, M., et al. (1995) Nat. Struct. Biol. 2, 504-509]. Finally, our study clearly demonstrates the powerful combination of NMR and SAXS in the study of modular proteins, since this enables reliable evaluation of both short-range (NMR) and long-range interactions (SAXS).

  • How an epidermal growth Factor (EGF)-like domain binds calcium. High resolution NMR structure of the calcium form of the NH2-terminal EGF-like domain in Coagulation Factor X.
    The Journal of biological chemistry, 1992
    Co-Authors: Maria Selander-sunnerhagen, Egon Persson, Johan Stenflo, Magnus Ullner, Olle Teleman, Torbjörn Drakenberg
    Abstract:

    Domains homologous to the epidermal growth Factor (EGF) are important building blocks for eXtracellular proteins. Proteins containing these domains have been shown to function in such diverse biological processes as blood Coagulation, complement activation, and the developmental determination of embryonic cell fates. Many of these proteins require calcium for their biological function. In the case of Coagulation Factors IX and X and anticoagulants proteins C and S, calcium has been found to bind to the EGF-like domains. We have now determined the three-dimensional structure of the calcium-bound form of the NH2-terminal EGF-like domain in Coagulation Factor X by two-dimensional NMR and simulated folding. Ligands to the calcium ion are the two backbone carbonyls in Gly-47 and Gly-64, as well as the side chains in Gln-49, erythro-beta-hydroXyaspartic acid (Hya) 63, and possibly Asp-46. The conserved Asp-48 is not a ligand in our present structures. The remaining ligands are assumed to be solvent molecules or, in the intact protein, ligands from neighboring domains. Other proteins interacting in a calcium-dependent manner may also contribute ligands. A comparison with the calcium-free form shows that calcium binding induces strictly local structural changes in the domain. Residues corresponding to the side chain ligands in Factor X are conserved in many other proteins, such as the integral membrane protein TAN-1 of human lymphocytes and its developmentally important homolog, Notch, in Drosophila. Calcium binding to EGF-like domains may be crucial for numerous protein-protein interactions involving EGF-like domains in Coagulation Factors, plasma proteins, and membrane proteins. Therefore, there is reason to believe that this novel calcium site plays an important role in the biochemistry of eXtracellular proteins.

  • Three-dimensional structure of the apo form of the N-terminal EGF-like module of blood Coagulation Factor X as determined by NMR spectroscopy and simulated folding.
    Biochemistry, 1992
    Co-Authors: Magnus Ullner, Egon Persson, Johan Stenflo, Torbjörn Drakenberg, Maria Selander, Olle Teleman
    Abstract:

    The three-dimensional structure of a 42-residue fragment containing the N-terminal EGF-like module of blood Coagulation Factor X was determined by means of 2D NMR spectroscopy and computer simulation. The spectroscopic data consisted of 370 NOE distances and 27 dihedral angle constraints. These were used to generate peptide conformations by molecular dynamics simulation. The simulations used a novel functional form for the constraint potentials and were performed with two time steps to ensure rapid eXecution. Apart from preliminary runs to aid assignment of NOEs, 60 runs resulted in 13 accepted structures, which have two antiparallel beta sheets, no alpha helices, and five tight turns. There is no hydrophobic cluster. The root mean square deviation for the backbone of the 13 conformations is 0.65 +/- 0.11 A against their mean conformation. About half of the side chains have well-defined structure. The overall conformation is similar to that of murine EGF.

Jesu Arockiaraj - One of the best experts on this subject based on the ideXlab platform.

  • Coagulation profile gene eXpression and bioinformatics characterization of Coagulation Factor X of striped murrel channa striatus
    Fish & Shellfish Immunology, 2016
    Co-Authors: Akila Sathyamoorthi, Abirami Arasu, Mariadhas Valan Arasu, Venkatesh Kumaresan, Naif Abdullah Aldhabi, Jesu Arockiaraj
    Abstract:

    A transcriptome wide analysis of the constructed cDNA library of snakehead murrel Channa striatus revealed a full length cDNA sequence of Coagulation Factor X. Sequence analysis of C. striatus Coagulation Factor X (CsFX) showed that the cDNA contained 1232 base pairs (bp) comprising 1209 bp open reading frame (ORF). The ORF region encodes 424 amino acids with a molecular mass of 59 kDa. The polypeptide contains γ-carboXyglutamic acid (GLA) rich domain and two epidermal growth Factor (EGF) like domains including EGF-CA domain and serine proteases trypsin signature profile. CsFX eXhibited the maXimum similarity with fish species such as Stegastes partitus (78%), Poecilia formosa (76%) and Cynoglossus semilaevis (74%). Phylogenetically, CsFX is clustered together with the fish group belonging to Actinopterygii. Secondary structure of Factor X includes alpha heliX 28.54%, eXtended strand 20.75%, beta turn 7.78% and random coil 42.92%. A predicted 3D model of CsFX revealed a short α-heliX and a Ca(2+) (Gla domain) binding site in the coil. Four disulfide bridges were found in serine protease trypsin profile. Obviously, the highest gene eXpression (P < 0.05) was noticed in blood. Further, the changes in eXpression of CsFX was observed after inducing with bacterial (Aeromonas hydrophila) and fungal (Aphanomyces invadans) infections and other synthetic immune stimulants. Variation in blood clotting time (CT), prothrombin time (PT) and activated prothromboplastin time (APTT) was analyzed and compared between healthy and bacterial infected fishes. During infection, PT and APTT showed a declined clotting time due to the raised level of thrombocytes.

  • Coagulation profile, gene eXpression and bioinformatics characterization of Coagulation Factor X of striped murrel Channa striatus
    Fish & Shellfish Immunology, 2016
    Co-Authors: Abirami Arasu, Akila Sathyamoorthi, Vellaisamy Kumaresan, Naif Abdullah Al-dhabi, Mariadhas Valan Arasu, Jesu Arockiaraj
    Abstract:

    Abstract A transcriptome wide analysis of the constructed cDNA library of snakehead murrel Channa striatus revealed a full length cDNA sequence of Coagulation Factor X. Sequence analysis of C . striatus Coagulation Factor X ( Cs FX) showed that the cDNA contained 1232 base pairs (bp) comprising 1209 bp open reading frame (ORF). The ORF region encodes 424 amino acids with a molecular mass of 59 kDa. The polypeptide contains γ-carboXyglutamic acid (GLA) rich domain and two epidermal growth Factor (EGF) like domains including EGF-CA domain and serine proteases trypsin signature profile. Cs FX eXhibited the maXimum similarity with fish species such as Stegastes partitus (78%), Poecilia formosa (76%) and Cynoglossus semilaevis (74%). Phylogenetically, Cs FX is clustered together with the fish group belonging to Actinopterygii . Secondary structure of Factor X includes alpha heliX 28.54%, eXtended strand 20.75%, beta turn 7.78% and random coil 42.92%. A predicted 3D model of Cs FX revealed a short α-heliX and a Ca 2+ (Gla domain) binding site in the coil. Four disulfide bridges were found in serine protease trypsin profile. Obviously, the highest gene eXpression (P  Cs FX was observed after inducing with bacterial ( Aeromonas hydrophila ) and fungal ( Aphanomyces invadans ) infections and other synthetic immune stimulants. Variation in blood clotting time (CT), prothrombin time (PT) and activated prothromboplastin time (APTT) was analyzed and compared between healthy and bacterial infected fishes. During infection, PT and APTT showed a declined clotting time due to the raised level of thrombocytes.

  • Coagulation profile, gene eXpression and bioinformatics characterization of Coagulation Factor X of striped murrel Channa striatus.
    Fish & shellfish immunology, 2016
    Co-Authors: Abirami Arasu, Akila Sathyamoorthi, Naif Abdullah Al-dhabi, Mariadhas Valan Arasu, Venkatesh Kumaresan, Jesu Arockiaraj
    Abstract:

    A transcriptome wide analysis of the constructed cDNA library of snakehead murrel Channa striatus revealed a full length cDNA sequence of Coagulation Factor X. Sequence analysis of C. striatus Coagulation Factor X (CsFX) showed that the cDNA contained 1232 base pairs (bp) comprising 1209 bp open reading frame (ORF). The ORF region encodes 424 amino acids with a molecular mass of 59 kDa. The polypeptide contains γ-carboXyglutamic acid (GLA) rich domain and two epidermal growth Factor (EGF) like domains including EGF-CA domain and serine proteases trypsin signature profile. CsFX eXhibited the maXimum similarity with fish species such as Stegastes partitus (78%), Poecilia formosa (76%) and Cynoglossus semilaevis (74%). Phylogenetically, CsFX is clustered together with the fish group belonging to Actinopterygii. Secondary structure of Factor X includes alpha heliX 28.54%, eXtended strand 20.75%, beta turn 7.78% and random coil 42.92%. A predicted 3D model of CsFX revealed a short α-heliX and a Ca(2+) (Gla domain) binding site in the coil. Four disulfide bridges were found in serine protease trypsin profile. Obviously, the highest gene eXpression (P 

Jill Trewhella - One of the best experts on this subject based on the ideXlab platform.

  • the relative orientation of gla and egf domains in Coagulation Factor X is altered by ca2 binding to the first egf domain a combined nmr small angle X ray scattering study
    Biochemistry, 1996
    Co-Authors: Maria Sunnerhagen, Johan Stenflo, Torbjörn Drakenberg, G A Olah, Sture Forsen, Jill Trewhella
    Abstract:

    Coagulation Factor X is a serine protease containing three noncatalytic domains:  an N-terminal γ-carboXyglutamic acid (Gla)1 domain followed by two epidermal growth Factor (EGF)-like domains. The isolated N-terminal EGF domain binds Ca2+ with a Kd of 10-3 M. When linked to the Gla domain, however, its Ca2+ affinity is increased 10-fold. In this paper, we present the NMR solution structure of the Factor X Gla−EGF domain pair with Ca2+ bound to the EGF domain, as well as small angle X-ray scattering (SAXS) data on the Gla−EGF domain pair with and without Ca2+. Our results show that Ca2+ binding to the EGF domain makes the Gla and EGF domains fold toward each other using the Ca2+ site as a hinge. Presumably, a similar mechanism may be responsible for alterations in the relative orientation of protein domains in many other eXtracellular proteins containing EGF domains with the consensus for Ca2+ binding. The results of the NMR and SAXS measurements reported in this paper confirm our previous result that the ...

  • The relative orientation of Gla and EGF domains in Coagulation Factor X is altered by Ca2+ binding to the first EGF domain. A combined NMR-small angle X-ray scattering study.
    Biochemistry, 1996
    Co-Authors: Maria Sunnerhagen, Johan Stenflo, Torbjörn Drakenberg, G A Olah, Sture Forsen, Jill Trewhella
    Abstract:

    Coagulation Factor X is a serine protease containing three noncatalytic domains: an N-terminal gamma-carboXyglutamic acid (Gla)1 domain followed by two epidermal growth Factor (EGF)-like domains. The isolated N-terminal EGF domain binds Ca2+ with a Kd of 10(-3) M. When linked to the Gla domain, however, its Ca2+ affinity is increased 10-fold. In this paper, we present the NMR solution structure of the Factor X Gla-EGF domain pair with Ca2+ bound to the EGF domain, as well as small angle X-ray scattering (SAXS) data on the Gla-EGF domain pair with and without Ca2+. Our results show that Ca2+ binding to the EGF domain makes the Gla and EGF domains fold toward each other using the Ca2+ site as a hinge. Presumably, a similar mechanism may be responsible for alterations in the relative orientation of protein domains in many other eXtracellular proteins containing EGF domains with the consensus for Ca2+ binding. The results of the NMR and SAXS measurements reported in this paper confirm our previous result that the Gla domain is folded also in its apo state when linked to the EGF domain [Sunnerhagen, M., et al. (1995) Nat. Struct. Biol. 2, 504-509]. Finally, our study clearly demonstrates the powerful combination of NMR and SAXS in the study of modular proteins, since this enables reliable evaluation of both short-range (NMR) and long-range interactions (SAXS).

Abirami Arasu - One of the best experts on this subject based on the ideXlab platform.

  • Coagulation profile gene eXpression and bioinformatics characterization of Coagulation Factor X of striped murrel channa striatus
    Fish & Shellfish Immunology, 2016
    Co-Authors: Akila Sathyamoorthi, Abirami Arasu, Mariadhas Valan Arasu, Venkatesh Kumaresan, Naif Abdullah Aldhabi, Jesu Arockiaraj
    Abstract:

    A transcriptome wide analysis of the constructed cDNA library of snakehead murrel Channa striatus revealed a full length cDNA sequence of Coagulation Factor X. Sequence analysis of C. striatus Coagulation Factor X (CsFX) showed that the cDNA contained 1232 base pairs (bp) comprising 1209 bp open reading frame (ORF). The ORF region encodes 424 amino acids with a molecular mass of 59 kDa. The polypeptide contains γ-carboXyglutamic acid (GLA) rich domain and two epidermal growth Factor (EGF) like domains including EGF-CA domain and serine proteases trypsin signature profile. CsFX eXhibited the maXimum similarity with fish species such as Stegastes partitus (78%), Poecilia formosa (76%) and Cynoglossus semilaevis (74%). Phylogenetically, CsFX is clustered together with the fish group belonging to Actinopterygii. Secondary structure of Factor X includes alpha heliX 28.54%, eXtended strand 20.75%, beta turn 7.78% and random coil 42.92%. A predicted 3D model of CsFX revealed a short α-heliX and a Ca(2+) (Gla domain) binding site in the coil. Four disulfide bridges were found in serine protease trypsin profile. Obviously, the highest gene eXpression (P < 0.05) was noticed in blood. Further, the changes in eXpression of CsFX was observed after inducing with bacterial (Aeromonas hydrophila) and fungal (Aphanomyces invadans) infections and other synthetic immune stimulants. Variation in blood clotting time (CT), prothrombin time (PT) and activated prothromboplastin time (APTT) was analyzed and compared between healthy and bacterial infected fishes. During infection, PT and APTT showed a declined clotting time due to the raised level of thrombocytes.

  • Coagulation profile, gene eXpression and bioinformatics characterization of Coagulation Factor X of striped murrel Channa striatus
    Fish & Shellfish Immunology, 2016
    Co-Authors: Abirami Arasu, Akila Sathyamoorthi, Vellaisamy Kumaresan, Naif Abdullah Al-dhabi, Mariadhas Valan Arasu, Jesu Arockiaraj
    Abstract:

    Abstract A transcriptome wide analysis of the constructed cDNA library of snakehead murrel Channa striatus revealed a full length cDNA sequence of Coagulation Factor X. Sequence analysis of C . striatus Coagulation Factor X ( Cs FX) showed that the cDNA contained 1232 base pairs (bp) comprising 1209 bp open reading frame (ORF). The ORF region encodes 424 amino acids with a molecular mass of 59 kDa. The polypeptide contains γ-carboXyglutamic acid (GLA) rich domain and two epidermal growth Factor (EGF) like domains including EGF-CA domain and serine proteases trypsin signature profile. Cs FX eXhibited the maXimum similarity with fish species such as Stegastes partitus (78%), Poecilia formosa (76%) and Cynoglossus semilaevis (74%). Phylogenetically, Cs FX is clustered together with the fish group belonging to Actinopterygii . Secondary structure of Factor X includes alpha heliX 28.54%, eXtended strand 20.75%, beta turn 7.78% and random coil 42.92%. A predicted 3D model of Cs FX revealed a short α-heliX and a Ca 2+ (Gla domain) binding site in the coil. Four disulfide bridges were found in serine protease trypsin profile. Obviously, the highest gene eXpression (P  Cs FX was observed after inducing with bacterial ( Aeromonas hydrophila ) and fungal ( Aphanomyces invadans ) infections and other synthetic immune stimulants. Variation in blood clotting time (CT), prothrombin time (PT) and activated prothromboplastin time (APTT) was analyzed and compared between healthy and bacterial infected fishes. During infection, PT and APTT showed a declined clotting time due to the raised level of thrombocytes.

  • Coagulation profile, gene eXpression and bioinformatics characterization of Coagulation Factor X of striped murrel Channa striatus.
    Fish & shellfish immunology, 2016
    Co-Authors: Abirami Arasu, Akila Sathyamoorthi, Naif Abdullah Al-dhabi, Mariadhas Valan Arasu, Venkatesh Kumaresan, Jesu Arockiaraj
    Abstract:

    A transcriptome wide analysis of the constructed cDNA library of snakehead murrel Channa striatus revealed a full length cDNA sequence of Coagulation Factor X. Sequence analysis of C. striatus Coagulation Factor X (CsFX) showed that the cDNA contained 1232 base pairs (bp) comprising 1209 bp open reading frame (ORF). The ORF region encodes 424 amino acids with a molecular mass of 59 kDa. The polypeptide contains γ-carboXyglutamic acid (GLA) rich domain and two epidermal growth Factor (EGF) like domains including EGF-CA domain and serine proteases trypsin signature profile. CsFX eXhibited the maXimum similarity with fish species such as Stegastes partitus (78%), Poecilia formosa (76%) and Cynoglossus semilaevis (74%). Phylogenetically, CsFX is clustered together with the fish group belonging to Actinopterygii. Secondary structure of Factor X includes alpha heliX 28.54%, eXtended strand 20.75%, beta turn 7.78% and random coil 42.92%. A predicted 3D model of CsFX revealed a short α-heliX and a Ca(2+) (Gla domain) binding site in the coil. Four disulfide bridges were found in serine protease trypsin profile. Obviously, the highest gene eXpression (P