2pru | pdb_00002pru

NMR Structure of Human apoS100B at 10C

spinqualitylabelsall models 2pru, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2pru is a 2 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1b4c, 1cfp, 1nsh Gene: S100B (Homo sapiens) Resources: FirstGlance, OCA, RCSB, PDBsum 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 S100B is one of the best-characterized members of the calcium-signaling S100 protein family. Most S100 proteins are dimeric, with each monomer containing two EF-hand calcium-binding sites (EF1, EF2). S100B and other S100 proteins respond to calcium increases in the cell by coordinating calcium and undergoing a conformational change that allows them to interact with a variety of cellular targets. Although several three dimensional structures of S100 proteins are available in the calcium-free (apo-) state it has been observed that these structures appear to adopt a wide range of conformations in the EF2 site with respect to the positioning of helix III, the helix that undergoes the most dramatic calcium-induced conformational change. In this work, we have determined the structure of human apo-S100B at 10 degrees C to examine whether temperature might be responsible for these structural differences. Further, we have used this data, and other available apo-S100 structures, to show that despite the range of interhelical angles adopted in the apo-S100 structures, normal Gaussian distributions about the mean angles found in the structure of human apo-S100B are observed. This finding, only obvious from the analysis of all available apo-S100 proteins, provides direct structural evidence that helix III is a loosely packed helix. This is likely a necessary functional property of the S100 proteins that facilitates the calcium-induced conformational change of helix III. In contrast, the calcium-bound structures of the S100 proteins show significantly smaller variability in the interhelical angles. This shows that calcium binding to the S100 proteins causes not only a conformational change but results in a tighter distribution of helices within the EF2 calcium binding site required for target protein interactions. Proteins 2008. (c) 2008 Wiley-Liss, Inc. Analysis of the structure of human apo-S100B at low temperature indicates a unimodal conformational distribution is adopted by calcium-free S100 proteins.,Malik S, Revington M, Smith SP, Shaw GS Proteins. 2008 Apr 2;. PMID:18384084 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also S100 protein

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