The Experts below are selected from a list of 24618 Experts worldwide ranked by ideXlab platform
Vivian Cody - One of the best experts on this subject based on the ideXlab platform.
-
Thyroid Hormone Structure-activity relationships: molecular Structure of 3,5,3'-triiodothyropropionic acid.
Endocrine Research, 2009Co-Authors: Vivian CodyAbstract:The crystal and molecular Structures of 3,5,3′–triiodothyropropionic acid (T3 P), determined as an N-diethanolamine salt, were carried out and the results are compared with those of other thyroid Hormone Structures. These data show that T3P has an unusual conformation with the diphenyl ether bridge outside the range normally observed for other thyroactive acid Structures and has the largest deviations from the ideal skewed conformation predicted for 3,5–diiodothyroactive compounds. These conformational properties are not observed in the Structures of thyroformic or acetic acid analogues. Biochemical data indicate that thyropropionic acid analogue activity differs from that of other acid analogues which could imply that their metabolism and activity can be controlled differently from that of other Hormone metabolites.
-
Conformational analysis of erythrosine B (FD&C Red No. 3) and its comparison with thyroid Hormone Structures.
Endocrine Research, 2009Co-Authors: Vivian CodyAbstract:Erythrosine B, also known as FD&C Red No. 3, is a tetraiodofluorescein dye that is widely used as a biological stain and color additive in food and drugs. Recent data show that erythrosine B and Rose Bengal, its polychlorophenyl derivative, are potent inhibitors of both 5'-T4 and 5-T4 monoiododeiodinase activity. However, fluorescein, the nonhalogenated parent compound, has no effect on deiodinase activity. The X-ray crystal Structure of erythrosine B was determined to elucidate the structural basis for its competition with T4 for its Hormone protein binding sites. These structural results show that the dye crystallizes as a free acid-ethanol solvate. The relative orientation of the benzoic acid and xanthine moieties is nearly perpendicular, similar to that observed in the Structure of fluorescein. As frequently noted in thyroid Hormone Structures, there are short I...I and I...O contact distances in this Structure. Because of the symmetric iodophenolic substitution pattern of the xanthine ring, there will always be one iodophenolic ring that is not homologous with the thyroid Hormone Structure. Therefore, this analysis suggests that the best conformational homology is achieved when the dye phenolic ring is matched with that of a skewed thyroid Hormone Structure.
Christian Cambillau - One of the best experts on this subject based on the ideXlab platform.
-
crystal Structure of a ternary complex between human chorionic gonadotropin hcg and two fv fragments specific for the alpha and beta subunits
Journal of Molecular Biology, 1999Co-Authors: Mariella Tegoni, S Spinelli, Martine Elisa Verhoeyen, Paul K Davis, Christian CambillauAbstract:Abstract Human chorionic gonadotropin (hCG), is a placental Hormone which exerts its major effect by stimulating progesterone production, crucially sustaining the early weeks of pregnancy. Detection of hCG with specific monoclonal antibodies (mAbs) has become the chosen means for pregnancy diagnosis. We have used antibody Fv fragments derived from two high-affinity mAbs, one against the α and the other against the β-hCG subunit to enable the crystallisation of intact or desialylated hCG. Crystals of a ternary complex composed of Fv anti-α/hCG/Fv anti-β were found to diffract to 3.5 A resolution, and the Structure was solved by molecular replacement. In the crystal, the two Fvs keep hCG as in a molecular cage, providing good protein-protein contacts and leaving enough space for the saccharides to be accommodated in the cell solvent. The two Fvs were found not to interact directly through their complementary-determining regions with the hCG saccharides, but only with the protein. The hCG Structure in the ternary complex was very close to that of the HF partially deglycosylated Hormone, thus indicating that neither the saccharides nor the Fvs had any substantial influence on Hormone Structure.
-
Crystal Structure of a ternary complex between human chorionic gonadotropin (hCG) and two Fv fragments specific for the alpha and beta-subunits.
Journal of Molecular Biology, 1999Co-Authors: Mariella Tegoni, S Spinelli, Martine Elisa Verhoeyen, Paul K Davis, Christian CambillauAbstract:Human chorionic gonadotropin (hCG), is a placental Hormone which exerts its major effect by stimulating progesterone production, crucially sustaining the early weeks of pregnancy. Detection of hCG with specific monoclonal antibodies (mAbs) has become the chosen means for pregnancy diagnosis. We have used antibody Fv fragments derived from two high-affinity mAbs, one against the alpha and the other against the beta-hCG subunit to enable the crystallisation of intact or desialylated hCG. Crystals of a ternary complex composed of Fv anti-alpha/hCG/Fv anti-beta were found to diffract to 3.5 A resolution, and the Structure was solved by molecular replacement. In the crystal, the two Fvs keep hCG as in a molecular cage, providing good protein-protein contacts and leaving enough space for the saccharides to be accommodated in the cell solvent. The two Fvs were found not to interact directly through their complementary-determining regions with the hCG saccharides, but only with the protein. The hCG Structure in the ternary complex was very close to that of the HF partially deglycosylated Hormone, thus indicating that neither the saccharides nor the Fvs had any substantial influence on Hormone Structure.
Mariella Tegoni - One of the best experts on this subject based on the ideXlab platform.
-
crystal Structure of a ternary complex between human chorionic gonadotropin hcg and two fv fragments specific for the alpha and beta subunits
Journal of Molecular Biology, 1999Co-Authors: Mariella Tegoni, S Spinelli, Martine Elisa Verhoeyen, Paul K Davis, Christian CambillauAbstract:Abstract Human chorionic gonadotropin (hCG), is a placental Hormone which exerts its major effect by stimulating progesterone production, crucially sustaining the early weeks of pregnancy. Detection of hCG with specific monoclonal antibodies (mAbs) has become the chosen means for pregnancy diagnosis. We have used antibody Fv fragments derived from two high-affinity mAbs, one against the α and the other against the β-hCG subunit to enable the crystallisation of intact or desialylated hCG. Crystals of a ternary complex composed of Fv anti-α/hCG/Fv anti-β were found to diffract to 3.5 A resolution, and the Structure was solved by molecular replacement. In the crystal, the two Fvs keep hCG as in a molecular cage, providing good protein-protein contacts and leaving enough space for the saccharides to be accommodated in the cell solvent. The two Fvs were found not to interact directly through their complementary-determining regions with the hCG saccharides, but only with the protein. The hCG Structure in the ternary complex was very close to that of the HF partially deglycosylated Hormone, thus indicating that neither the saccharides nor the Fvs had any substantial influence on Hormone Structure.
-
Crystal Structure of a ternary complex between human chorionic gonadotropin (hCG) and two Fv fragments specific for the alpha and beta-subunits.
Journal of Molecular Biology, 1999Co-Authors: Mariella Tegoni, S Spinelli, Martine Elisa Verhoeyen, Paul K Davis, Christian CambillauAbstract:Human chorionic gonadotropin (hCG), is a placental Hormone which exerts its major effect by stimulating progesterone production, crucially sustaining the early weeks of pregnancy. Detection of hCG with specific monoclonal antibodies (mAbs) has become the chosen means for pregnancy diagnosis. We have used antibody Fv fragments derived from two high-affinity mAbs, one against the alpha and the other against the beta-hCG subunit to enable the crystallisation of intact or desialylated hCG. Crystals of a ternary complex composed of Fv anti-alpha/hCG/Fv anti-beta were found to diffract to 3.5 A resolution, and the Structure was solved by molecular replacement. In the crystal, the two Fvs keep hCG as in a molecular cage, providing good protein-protein contacts and leaving enough space for the saccharides to be accommodated in the cell solvent. The two Fvs were found not to interact directly through their complementary-determining regions with the hCG saccharides, but only with the protein. The hCG Structure in the ternary complex was very close to that of the HF partially deglycosylated Hormone, thus indicating that neither the saccharides nor the Fvs had any substantial influence on Hormone Structure.
S Spinelli - One of the best experts on this subject based on the ideXlab platform.
-
crystal Structure of a ternary complex between human chorionic gonadotropin hcg and two fv fragments specific for the alpha and beta subunits
Journal of Molecular Biology, 1999Co-Authors: Mariella Tegoni, S Spinelli, Martine Elisa Verhoeyen, Paul K Davis, Christian CambillauAbstract:Abstract Human chorionic gonadotropin (hCG), is a placental Hormone which exerts its major effect by stimulating progesterone production, crucially sustaining the early weeks of pregnancy. Detection of hCG with specific monoclonal antibodies (mAbs) has become the chosen means for pregnancy diagnosis. We have used antibody Fv fragments derived from two high-affinity mAbs, one against the α and the other against the β-hCG subunit to enable the crystallisation of intact or desialylated hCG. Crystals of a ternary complex composed of Fv anti-α/hCG/Fv anti-β were found to diffract to 3.5 A resolution, and the Structure was solved by molecular replacement. In the crystal, the two Fvs keep hCG as in a molecular cage, providing good protein-protein contacts and leaving enough space for the saccharides to be accommodated in the cell solvent. The two Fvs were found not to interact directly through their complementary-determining regions with the hCG saccharides, but only with the protein. The hCG Structure in the ternary complex was very close to that of the HF partially deglycosylated Hormone, thus indicating that neither the saccharides nor the Fvs had any substantial influence on Hormone Structure.
-
Crystal Structure of a ternary complex between human chorionic gonadotropin (hCG) and two Fv fragments specific for the alpha and beta-subunits.
Journal of Molecular Biology, 1999Co-Authors: Mariella Tegoni, S Spinelli, Martine Elisa Verhoeyen, Paul K Davis, Christian CambillauAbstract:Human chorionic gonadotropin (hCG), is a placental Hormone which exerts its major effect by stimulating progesterone production, crucially sustaining the early weeks of pregnancy. Detection of hCG with specific monoclonal antibodies (mAbs) has become the chosen means for pregnancy diagnosis. We have used antibody Fv fragments derived from two high-affinity mAbs, one against the alpha and the other against the beta-hCG subunit to enable the crystallisation of intact or desialylated hCG. Crystals of a ternary complex composed of Fv anti-alpha/hCG/Fv anti-beta were found to diffract to 3.5 A resolution, and the Structure was solved by molecular replacement. In the crystal, the two Fvs keep hCG as in a molecular cage, providing good protein-protein contacts and leaving enough space for the saccharides to be accommodated in the cell solvent. The two Fvs were found not to interact directly through their complementary-determining regions with the hCG saccharides, but only with the protein. The hCG Structure in the ternary complex was very close to that of the HF partially deglycosylated Hormone, thus indicating that neither the saccharides nor the Fvs had any substantial influence on Hormone Structure.
Martine Elisa Verhoeyen - One of the best experts on this subject based on the ideXlab platform.
-
crystal Structure of a ternary complex between human chorionic gonadotropin hcg and two fv fragments specific for the alpha and beta subunits
Journal of Molecular Biology, 1999Co-Authors: Mariella Tegoni, S Spinelli, Martine Elisa Verhoeyen, Paul K Davis, Christian CambillauAbstract:Abstract Human chorionic gonadotropin (hCG), is a placental Hormone which exerts its major effect by stimulating progesterone production, crucially sustaining the early weeks of pregnancy. Detection of hCG with specific monoclonal antibodies (mAbs) has become the chosen means for pregnancy diagnosis. We have used antibody Fv fragments derived from two high-affinity mAbs, one against the α and the other against the β-hCG subunit to enable the crystallisation of intact or desialylated hCG. Crystals of a ternary complex composed of Fv anti-α/hCG/Fv anti-β were found to diffract to 3.5 A resolution, and the Structure was solved by molecular replacement. In the crystal, the two Fvs keep hCG as in a molecular cage, providing good protein-protein contacts and leaving enough space for the saccharides to be accommodated in the cell solvent. The two Fvs were found not to interact directly through their complementary-determining regions with the hCG saccharides, but only with the protein. The hCG Structure in the ternary complex was very close to that of the HF partially deglycosylated Hormone, thus indicating that neither the saccharides nor the Fvs had any substantial influence on Hormone Structure.
-
Crystal Structure of a ternary complex between human chorionic gonadotropin (hCG) and two Fv fragments specific for the alpha and beta-subunits.
Journal of Molecular Biology, 1999Co-Authors: Mariella Tegoni, S Spinelli, Martine Elisa Verhoeyen, Paul K Davis, Christian CambillauAbstract:Human chorionic gonadotropin (hCG), is a placental Hormone which exerts its major effect by stimulating progesterone production, crucially sustaining the early weeks of pregnancy. Detection of hCG with specific monoclonal antibodies (mAbs) has become the chosen means for pregnancy diagnosis. We have used antibody Fv fragments derived from two high-affinity mAbs, one against the alpha and the other against the beta-hCG subunit to enable the crystallisation of intact or desialylated hCG. Crystals of a ternary complex composed of Fv anti-alpha/hCG/Fv anti-beta were found to diffract to 3.5 A resolution, and the Structure was solved by molecular replacement. In the crystal, the two Fvs keep hCG as in a molecular cage, providing good protein-protein contacts and leaving enough space for the saccharides to be accommodated in the cell solvent. The two Fvs were found not to interact directly through their complementary-determining regions with the hCG saccharides, but only with the protein. The hCG Structure in the ternary complex was very close to that of the HF partially deglycosylated Hormone, thus indicating that neither the saccharides nor the Fvs had any substantial influence on Hormone Structure.