1b56

HUMAN RECOMBINANT EPIDERMAL FATTY ACID BINDING PROTEIN

spinqualitylabelsall models 1b56, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1b56 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PLM Resources: FirstGlance, OCA, RCSB, PDBsum Function [FABP5_HUMAN] High specificity for fatty acids. Highest affinity for C18 chain length. Decreasing the chain length or introducing double bonds reduces the affinity. May be involved in keratinocyte differentiation. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed We describe the crystal structure of human epidermal-type fatty acid binding protein (E-FABP) that was recently found to be highly upregulated in human psoriatic keratinocytes. To characterize E-FABP with respect to ligand-binding properties and tertiary structure, we cloned the respective cDNA, overexpressed the protein in Escherichia coli and purified it to homogeneity by a combination of ion-exchange and size-exclusion chromatographic steps with a yield of 30 mg/L broth. The purified protein revealed a 5-fold higher affinity for stearic acid than for oleic and arachidonic acids. The crystal structure of recombinant human E-FABP was determined to 2.05 A and refined to an R(factor) of 20.7%. The initial residual electron density maps clearly showed the presence of a ligand, which was identified as endogenous bacterial fatty acid. Within a central cavity of 252 A(3), this ligand is bound in a U-shaped conformation, its carboxyl group interacting with tyrosine 131 and arginines 129 and 109, the latter via an ordered water molecule. The E-FABP crystal structure is unique in the FABP family because of the presence of a disulfide bridge between cysteines 120 and 127 that may be physiologically as well as pathophysiologically relevant. Cysteines 67 and 87 are also in close vicinity but in contrast do not form a disulfide bridge. We postulate that this protein belongs to a particular FABP subfamily whose members share common structural as well as functional features. Expression, purification, and crystal structure determination of recombinant human epidermal-type fatty acid binding protein.,Hohoff C, Borchers T, Rustow B, Spener F, van Tilbeurgh H Biochemistry. 1999 Sep 21;38(38):12229-39. PMID:10493790 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Fatty acid-binding protein

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