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J F Glatz - One of the best experts on this subject based on the ideXlab platform.
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Fatty acid binding Proteins as plasma markers of tissue injury
Clinica Chimica Acta, 2005Co-Authors: Maurice M A L Pelsers, Wim Th Hermens, J F GlatzAbstract:Abstract Background One of the novel and promising plasma markers for detection of tissue injury is the family of 15 kDa cytoplasmic Fatty Acid-Binding Proteins of which various tissue-specific types occur. Aims and Objectives The present status of heart-type Fatty Acid-Binding protein (H-FABP) as a diagnostic and prognostic marker for acute and chronic cardiac injury, as well as the preliminary diagnostic use of other types of FABP for detecting injury in other organs, is reviewed. Methods This review is based on an overview of the literature on clinical diagnostics of various forms of organ injury, and uses additional literature on physiological aspects relevant for the interpretation of plasma marker concentrations. Results H-FABP not only proves to be an excellent early marker for cardiac injury in acute coronary syndromes, but also allows detection of minor myocardial injury in heart failure and unstable angina. Preliminary results indicate that sensitivity, rule-out power and prognostic value of H-FABP in cardiac injury surpass the performance of the standard early marker myoglobin. The liver only contains liver-type FABP (L-FABP), but co-expression of H-FABP and L-FABP occurs in the kidney. Similarly, intestinal-type FABP (I-FABP) and L-FABP are found in intestines, and brain-type FABP (B-FABP) and H-FABP occur in the brain. Preliminary but promising applications of these Proteins have been demonstrated for liver rejection, viability selection of kidneys from non-heart-beating donors (NHBD), inflammatory and ischemic bowel disease, traumatic brain injury and in the prevention of muscle injury in trained athletes. Conclusions Further study of the diagnostic and prognostic use of various FABP types is warranted, but their clinical application will require further commercialization of automated and rapid assays.
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Unravelling the significance of cellular Fatty Acid-Binding Proteins.
Current opinion in lipidology, 2001Co-Authors: J F Glatz, Judith StorchAbstract:Cellular long-chain Fatty acid (FA) transport and metabolism are believed to be regulated by membrane-associated and soluble Proteins that bind and transport FAs. Several different classes of membrane Proteins have been proposed as FA acceptors or transmembrane FA transporters. New evidence from in-vitro and whole-animal studies supports the existence of protein-mediated transmembrane transport of FAs, which is likely to coexist with passive diffusional uptake. The trafficking of FAs by intracellular Fatty Acid-Binding Proteins may involve their interaction with specific membrane or protein targets. Evidence is also emerging for concerted actions between the membrane and cytoplasmic Fatty Acid-Binding Proteins that allow for efficient regulation of FA transport and metabolism.
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Fatty Acid-Binding Proteins in the heart
Molecular and Cellular Biochemistry, 1998Co-Authors: Frank G. Schaap, Ger J. Van Der Vusse, J F GlatzAbstract:Long-chain Fatty acids are important fuel molecules for the heart, their oxidation in mitochondria providing the bulk of energy required for cardiac functioning. The low solubility of Fatty acids in aqueous solutions impairs their cellular transport. However, cardiac tissue contains several Proteins capable of binding Fatty acids non-covalently. These Fatty Acid-Binding Proteins (FABPs) are thought to facilitate both cellular uptake and intracellular transport of Fatty acids. The majority of Fatty acids taken up by the heart seems to pass the sarcolemma through a carrier-mediated translocation mechanism consisting of one or more membrane-associated FABPs. Intracellular transport of Fatty acids towards sites of metabolic conversion is most likely accomplished by cytoplasmic FABPs. In this review, the roles of membrane-associated and cytoplasmic FABPs in cardiac Fatty acid metabolism under (patho)physiological circumstances are discussed.
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Recombinant human heart-type Fatty Acid-Binding protein as standard in immunochemical assays.
Clinical chemistry and laboratory medicine, 1998Co-Authors: Andrea Schreiber, J F Glatz, Maurice M A L Pelsers, Torsten Börchers, Bernfried Specht, Friedrich SpenerAbstract:Cytoplasmic heart-type Fatty Acid-Binding protein has recently gained much attention in clinical diagnosis as a very early marker of acute myocardial infarction. Immunoassays have been developed for determination of this protein in plasma and urine samples. In the present study it is shown that those types of Fatty Acid-Binding Proteins which are abundant in tissues other than heart and muscle do not interfere with immunochemical determination of heart-type Fatty Acid-Binding protein. To provide sufficient protein of consistent quality as standard in these immunoassays, human heart-type Fatty Acid-Binding protein was cloned, expressed in Escherichia coli and purified to homogeneity. For quantitation of the recombinant protein its extinction coefficient was determined. Comparison of the recombinant and tissue-derived Proteins by a variety of methods revealed both Proteins to show similar kinetic as well as equilibrium constants with respect to two monoclonal antibodies currently applied in immunochemical detection of heart-type Fatty Acid-Binding protein. Both preparations were indistiguishable in sandwich-ELISA and immunosensor measurements. A high stability of the recombinant protein was proven by ELISA measurements during storage and several freeze and thaw cycles. Thus, recombinant and tissue-derived heart-type Fatty Acid-Binding Proteins are immunochemically equivalent. The recombinant human heart-type Fatty Acid-Binding protein is now available as standard for immunoassays.
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Membrane-associated and cytoplasmic Fatty Acid-Binding Proteins.
Lipids, 1996Co-Authors: F A Van Nieuwenhoven, G J Van Der Vusse, J F GlatzAbstract:A number of cellular Fatty Acid-Binding Proteins are being implicated in the uptake and intracellular transport of long-chain Fatty acids by parenchymal cells. Having been a topic of research for more than 20 years, cytoplasmic Fatty Acid-Binding Proteins now are assigned various pivotal functions in intracellular Fatty acid transport and metabolism. More recently several membrane-associated Fatty Acid-Binding Proteins have been identified and these Proteins are thought to function in the transmembrane transport of Fatty acids. In this review, a short summary is provided of the latest developments in this research area.
Friedrich Spener - One of the best experts on this subject based on the ideXlab platform.
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brain and heart type Fatty acid binding Proteins in the brain tissue distribution and clinical utility
Clinical Chemistry, 2004Co-Authors: Maurice M A L Pelsers, Friedrich Spener, Thorsten Hanhoff, Danielle Van Der Voort, Baer Arts, Maarten J V Peters, Rudolf W H M Ponds, Adriaan Honig, Wojtek Rudzinski, Jelle De KruijkAbstract:Background: Detection of brain injury by serum markers is not a standard procedure in clinical practice, although several Proteins, such as S100B, neuron-specific enolase (NSE), myelin basic protein, and glial fibrillary acidic protein, show promising results. We investigated the tissue distribution of brain- and heart-type Fatty Acid-Binding Proteins (B-FABP and H-FABP) in segments of the human brain and the potential of either protein to serve as plasma marker for diagnosis of brain injury. Methods: B-FABP and H-FABP were measured immunochemically in autopsy samples of the brain (n = 6) and in serum samples from ( a ) patients with mild traumatic brain injury (MTBI; n = 130) and ( b ) depressed patients undergoing bilateral electroconvulsive therapy (ECT; n = 14). The protein markers S100B and NSE were measured for comparison. Reference values of B-FABP and H-FABP were established in healthy individuals (n = 92). Results: The frontal, temporal, and occipital lobes, the striatum, the pons, and the cerebellum had different tissue concentrations of B-FABP and of H-FABP. B-FABP ranged from 0.8 μg/g wet weight in striatum tissue to 3.1 μg/g in frontal lobe. H-FABP was markedly higher, ranging from 16.2 μg/g wet weight in cerebellum tissue to 39.5 μg/g in pons. No B-FABP was detected in serum from healthy donors. H-FABP serum reference value was 6 μg/L. In the MTBI study, serum B-FABP was increased in 68% and H-FABP in 70% of patients compared with S100B (increased in 45%) and NSE (increased in 51% of patients). In ECT, serum B-FABP was increased in 6% of all samples (2 of 14 patients), whereas H-FABP was above its upper reference limit (6 μg/L) in 17% of all samples (8 of 14 patients), and S100B was above its upper reference limit (0.3 μg/L) in 0.4% of all samples. Conclusions: B-FABP and H-FABP patterns differ among brain tissues, with the highest concentrations in the frontal lobe and pons, respectively. However, in each part of the brain, the H-FABP concentration was at least 10 times higher than that of B-FABP. Patient studies indicate that B-FABP and H-FABP are more sensitive markers for minor brain injury than the currently used markers S100B and NSE.
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Insights into binding of Fatty acids by Fatty acid binding Proteins
Molecular and Cellular Biochemistry, 2002Co-Authors: Thorsten Hanhoff, Christian Lücke, Friedrich SpenerAbstract:Members of the phylogenetically related intracellular lipid binding protein (iLBP) are characterized by a highly conserved tertiary structure, but reveal distinct binding preferences with regard to ligand structure and conformation, when binding is assessed by the Lipidex method (removal of unbound ligand by hydrophobic polymer) or by isothermal titration calorimetry, a true equilibrium method. Subfamily Proteins bind retinoids, subfamily II Proteins bind bulky ligands, examples are intestinal bile acid binding protein (I-BABP) and liver Fatty acid binding protein (L-FABP) which binds 2 ligand molecules, preferably monounsaturated and n-3 Fatty acids. Subfamily III intestinal Fatty acid binding protein (I-FABP) binds Fatty acid in a bent conformation. The Fatty acid bound by subfamily IV FABPs has a U-shaped conformation; here heart (H-) FABP preferably binds n-6, brain (B-) FABP n-3 Fatty acids. The ADIFAB-method is a fluorescent test for Fatty acid in equilibrium with iLBP and reveals some correlation of binding affinity to Fatty acid solubility in the aqueous phase; these data are often at variance with those obtained by the other methods. Thus, in this review published binding data are critically discussed, taking into account on the one hand binding increments calculated for Fatty acid double bonds on the basis of the ‘solubility’ hypothesis, on the other hand the interpretation of calorimetric data on the basis of crystallographic and solution structures of iLBPs.
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Recombinant human heart-type Fatty Acid-Binding protein as standard in immunochemical assays.
Clinical chemistry and laboratory medicine, 1998Co-Authors: Andrea Schreiber, J F Glatz, Maurice M A L Pelsers, Torsten Börchers, Bernfried Specht, Friedrich SpenerAbstract:Cytoplasmic heart-type Fatty Acid-Binding protein has recently gained much attention in clinical diagnosis as a very early marker of acute myocardial infarction. Immunoassays have been developed for determination of this protein in plasma and urine samples. In the present study it is shown that those types of Fatty Acid-Binding Proteins which are abundant in tissues other than heart and muscle do not interfere with immunochemical determination of heart-type Fatty Acid-Binding protein. To provide sufficient protein of consistent quality as standard in these immunoassays, human heart-type Fatty Acid-Binding protein was cloned, expressed in Escherichia coli and purified to homogeneity. For quantitation of the recombinant protein its extinction coefficient was determined. Comparison of the recombinant and tissue-derived Proteins by a variety of methods revealed both Proteins to show similar kinetic as well as equilibrium constants with respect to two monoclonal antibodies currently applied in immunochemical detection of heart-type Fatty Acid-Binding protein. Both preparations were indistiguishable in sandwich-ELISA and immunosensor measurements. A high stability of the recombinant protein was proven by ELISA measurements during storage and several freeze and thaw cycles. Thus, recombinant and tissue-derived heart-type Fatty Acid-Binding Proteins are immunochemically equivalent. The recombinant human heart-type Fatty Acid-Binding protein is now available as standard for immunoassays.
Judith Storch - One of the best experts on this subject based on the ideXlab platform.
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similar mechanisms of Fatty acid transfer from human anal rodent Fatty acid binding Proteins to membranes liver intestine heart muscle and adipose tissue fabps
Molecular and Cellular Biochemistry, 2002Co-Authors: Judith Storch, J H Veerkamp, Kuotung HsuAbstract:The mammalian Fatty Acid-Binding Proteins (FABPs) are thought to be important for the transport and metabolism of Fatty acids in numerous cell types. The transfer of FA from different members of the FABP family to membranes has been shown to occur by two distinct mechanisms, an aqueous diffusion-based mechanism and a collisional mechanism, wherein the FABP interacts directly with membrane acceptors. Much of the work that underlies this concept comes from efforts using rodent FABPs. Given the increasing awareness of links between FABPs and several chronic diseases in humans, it was important to establish the mechanisms of FA transfer for human FABPs. In the present studies, we examined the rate and mechanism of Fatty acid transfer from four pairs of human and rodent (rat or mouse, as specified) FABPs: hLFABP and rLFABP, hIFABP and rIFABP, hHFABP and rHFABP, and hAFABP and mAFABP. In the case of human IFABP, both the Ala54 and Thr54 forms were examined. The results show clearly that for all FABPs examined, the mechanisms of ligand transfer observed for rodent Proteins hold true for their human counterparts. Moreover, it appears that the Ala to Thr substitution at residue 54 of the human IFABP does not alter the fundamental mechanism of ligand transfer to membranes, but nevertheless causes a consistent decrease in the rate of transfer.
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Unravelling the significance of cellular Fatty Acid-Binding Proteins.
Current opinion in lipidology, 2001Co-Authors: J F Glatz, Judith StorchAbstract:Cellular long-chain Fatty acid (FA) transport and metabolism are believed to be regulated by membrane-associated and soluble Proteins that bind and transport FAs. Several different classes of membrane Proteins have been proposed as FA acceptors or transmembrane FA transporters. New evidence from in-vitro and whole-animal studies supports the existence of protein-mediated transmembrane transport of FAs, which is likely to coexist with passive diffusional uptake. The trafficking of FAs by intracellular Fatty Acid-Binding Proteins may involve their interaction with specific membrane or protein targets. Evidence is also emerging for concerted actions between the membrane and cytoplasmic Fatty Acid-Binding Proteins that allow for efficient regulation of FA transport and metabolism.
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The Fatty acid transport function of Fatty Acid-Binding Proteins.
Biochimica et Biophysica Acta, 2000Co-Authors: Judith Storch, Alfred E. ThumserAbstract:The intracellular Fatty Acid-Binding Proteins (FABPs) comprise a family of 14–15 kDa Proteins which bind long-chain Fatty acids. A role for FABPs in Fatty acid transport has been hypothesized for several decades, and the accumulated indirect and correlative evidence is largely supportive of this proposed function. In recent years, a number of experimental approaches which more directly examine the transport function of FABPs have been taken. These include molecular level in vitro modeling of Fatty acid transfer mechanisms, whole cell studies of Fatty acid uptake and intracellular transfer following genetic manipulation of FABP type and amount, and an examination of cells and tissues from animals engineered to lack expression of specific FABPs. Collectively, data from these studies have provided strong support for defining the FABPs as Fatty acid transport Proteins. Further studies are necessary to elucidate the fundamental mechanisms by which cellular Fatty acid trafficking is modulated by the FABPs.
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Binding site polarity and ligand affinity of homologous Fatty Acid-Binding Proteins from animals with different body temperatures
Molecular and Cellular Biochemistry, 1996Co-Authors: Richard L. Londraville, Judith Storch, Bruce D. SidellAbstract:Binding affinity and binding-pocket polarity is determined for intracellular Fatty acid- binding protein (FABP) from aerobic muscle of Chaenocephalus aceratus , the Antarctic icefish, and from rat heart. FABPs bind Fatty acids via weak-bond forces (both ionic and hydrophobic), and these bond forces are temperature sensitive, yet FABPs are present in animals whose body temperatures range over nearly 40°C. To investigate FABPs sensitivity to body temperature, Fatty acid binding affinity (K_d) was determined for both rat heart-FABP and icefish heart-FABP at two physiological temperatures (0°C or 37°C). Saturated and unsaturated Fatty acids (16:0 and 16:1), delivered in model membranes (liposomes) whose composition is typical of either Antarctic fish (16:0/22:6 phosphatidylcholine) or mammals (bovine-heart phosphatidylcholine) were examined. Incubation at 0°C or 37°C does not significantly affect K_d for rat heart FABP, regardless of liposome composition or Fatty acid ligand (K_d = 0.686 ± 0.127 – 1.129 ± 0.356 μM at 0°C, 0.775 ± 0.307 – 1.605 ± 0.427 gM at 37°C). Incubation temperature significantly affects icefish FABPs affinity for 16:1 (0.626 ± 0.093 μM at 37°C vs. 1.896 ± 0.343 μM at 0°C for Fatty acid presented in Antarctic fish liposomes; 0.331 ± 0.101 μM at 37°C vs. 0.949 ± 0.121 μM at 0°C for bovine heart liposomes) but not 16:0. K_d is not significantly different between FABPs under any set of conditions (with one exception: K_d is significantly lower in rat FABP vs. icefish FABP for 16:0 at 0°C for Fatty acids delivered in bovine heart liposomes). Although K_d values are largely equivalent between the two FABPs, relative contributions from ionic vs. hydrophobic weak-bond forces are different between the two animals. Rat heart FABP has a binding pocket that is significantly more nonpolar than that of icefish FABP (as measured by quantum yield of the bound fluorescent Fatty-acid analogue (PA-DPH); Q = 0.067 ± 0.008 vs. 0.034 ± 0.005 at 0°C, 0.030 ± 0.003 vs. 0.019 ± 0.002 at 37°C). This suggests that rat-heart FABP realizes a micromolar Kd with a greater reliance upon hydrophobic interactions than does icefish FABP.
José A. Santomé - One of the best experts on this subject based on the ideXlab platform.
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A Fatty Acid-Binding protein and a protein disulphide isomerase-related protein expressed in urochordate gonad cytosol.
The International Journal of Biochemistry & Cell Biology, 2000Co-Authors: Brian M Cavagnari, Graciela B. Esnal, Ricardo Sahade, Marcos Tatian, José A. SantoméAbstract:Abstract Despite the evolutionary-tree data suggesting that gene duplication leading to the divergence of the three branches which heart, liver and intestinal Fatty Acid-Binding Proteins belong to must have occurred before the vertebrate/invertebrate split, only the heart Fatty Acid-Binding protein has been reported for invertebrates. In an attempt to shed light on this apparent inconsistency the presence of the other two branch members was investigated in the Urochordata Molgula pedunculata , an ascidian species close to vertebrates. The mantle-, gonad- and digestive tube-cytosolic fractions, obtained by centrifugation at 106,000 g , were incubated separately with [1- 14 C]palmitic acid and then fractionated on a Sephadex G-75 column. In the case of gonads and digestive tube, radioactive peaks corresponding to a molecular mass of 14–16 kDa, characteristic of Fatty Acid-Binding Proteins, were detected. When the experiment was performed on the mantle, this peak showing Fatty acid binding capacity was absent. Western Blot of the radioactive 14–16 kDa Sephadex fraction from the urochordate gonad cross-reacted with rat liver Fatty Acid-Binding protein anti-serum but did not do so with anti-rat intestinal, adipocyte or heart Fatty Acid-Binding protein antisera. The material from the digestive tube was not recognized by any of the antisera. The most abundant protein in said 14–16 kDa fraction was a protein disulphide isomerase-related protein. Its partial amino acid sequence was determined.
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Presence of intestinal, liver and heart/adipocyte Fatty-Acid-Binding protein types in the liver of a chimaera fish
The international journal of biochemistry & cell biology, 1998Co-Authors: Osvaldo L. Córdoba, Jacques H. Veerkamp, Eduardo I. Sánchez, José A. SantoméAbstract:Abstract Five Fatty-Acid-Binding Proteins from the liver of the elephant fish (Callorhynchus callorhynchus), a chimaera fish that belongs—together with the elasmobranchs—to the ancient chondrichthyes class were isolated and characterized. The purification procedures for these Proteins involved gel filtration, anion-exchange chromatography, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis as a last step. They were submitted to “in gel” tryptic or cyanogen bromide digestion and the resulting peptides were separated by high performance liquid chromatography and then sequenced by Edman degradation. According to their partial amino acid sequences, one of them presents the highest identity with Fatty-Acid-Binding Proteins from human and catfish liver, another three with those from mammalian heart or adipose tissue and the fifth with the mammalian intestinal Fatty-Acid-Binding protein. The presence of various members of this protein family, as now found in elephant fish and previously in catfish (Rhamdia sapo) liver, does not occur in mammalian liver which expresses only one a characteristic Fatty-Acid-Binding protein.
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Purification, characterization and partial sequencing of the heart Fatty Acid-Binding protein from Bufo arenarum
Comparative biochemistry and physiology. Biochemistry and molecular biology, 1994Co-Authors: Christian H. Schleicher, José A. SantoméAbstract:A 15.7 kDa Fatty Acid-Binding protein from toad heart was purified by gel-filtration chromatography on Sephadex G-75 followed by anion-exchange chromatography on a Mono-Q column. Purity was confirmed by gel electrophoresis and isoelectric focusing. Molecular mass, isoelectric point, amino acid composition and partial internal sequence showed that the protein is related to mammalian heart Fatty Acid-Binding Proteins.
Darren R Flower - One of the best experts on this subject based on the ideXlab platform.
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the lipocalin protein family structural and sequence overview
Biochimica et Biophysica Acta, 2000Co-Authors: Darren R Flower, Anthony C.t. North, Clare SansomAbstract:Abstract Lipocalins are remarkably diverse at the sequence level yet have highly conserved structures. Most lipocalins share three characteristic conserved sequence motifs – the kernel lipocalins – while others are more divergent family members – the outlier lipocalins – typically sharing only one or two. This classification is a useful tool for analysing the family, and within these large sets are smaller groups sharing much higher levels of sequence similarity. The lipocalins are also part of a larger protein superfamily: the calycins, which includes the Fatty acid binding Proteins, avidins, a group of metalloproteinase inhibitors, and triabin. The superfamily is characterised by a similar structure (a repeated +1 topology β-barrel) and by the conservation of a remarkable structural signature.
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The lipocalin protein family: structural and sequence overview.
Biochimica et biophysica acta, 2000Co-Authors: Darren R Flower, Anthony C.t. North, Clare SansomAbstract:Lipocalins are remarkably diverse at the sequence level yet have highly conserved structures. Most lipocalins share three characteristic conserved sequence motifs - the kernel lipocalins - while others are more divergent family members - the outlier lipocalins - typically sharing only one or two. This classification is a useful tool for analysing the family, and within these large sets are smaller groups sharing much higher levels of sequence similarity. The lipocalins are also part of a larger protein superfamily: the calycins, which includes the Fatty acid binding Proteins, avidins, a group of metalloproteinase inhibitors, and triabin. The superfamily is characterised by a similar structure (a repeated +1 topology beta-barrel) and by the conservation of a remarkable structural signature.
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Structural relationship of streptavidin to the calycin protein superfamily.
FEBS letters, 1993Co-Authors: Darren R FlowerAbstract:Streptavidin is a binding protein, from the bacteria Streptomyces avidinii, with remarkable affinity for the vitamin biotin. The lipocalins and the Fatty Acid-Binding Proteins (FABPs), are two other protein families which also act by binding small hydrophobic molecules. Within a similar overall folding pattern (a beta-barrel with a repeated +1 topology), large parts of the lipocalin, FABP, and streptavidin molecules can be structurally equivalenced. The first structurally conserved region within the three-dimensional alignment, or common core, characteristic of the three groups corresponds to an unusual structural feature (a short 3(10) helix leading into a beta-strand, the first of the barrel), conserved in both its conformation and its location within their folds, which also displays characteristic sequence conservation. These similarities of structure and sequence suggest that all three families form part of a larger group: the calycin structural superfamily.
