2h2k
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Crystal Structure Analysis of Human S100A13
OverviewOverview
The S100 protein family is the largest group of calcium-binding protein, families, which consists of at least 25 members. S100A13, which is widely, expressed in a variety of tissues, is a unique member of the S100 protein, family. Previous reports showed that S100A13 might be involved in the, stress-induced release of some signal peptide-less proteins (such as FGF-1, and IL-1alpha) and also associated with inflammatory functions. It was, also reported that S100A13 is a new angiogenesis marker. Here we report, the crystal structure of the Ca(2+)-bound form of S100A13 at 2.0 A, resolution. S100A13 is a homodimer with four EF-hand motifs in an, asymmetric unit, displaying a folding pattern similar to other S100, members. However, S100A13 has the unique structural feature with all, alpha-helices being amphiphilic, which was not found in other members of, S100s. We propose that this characteristic structure of S100A13 might be, related to its ability to mediate the release of FGF-1 and IL-1alpha.
About this StructureAbout this Structure
2H2K is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure study on human S100A13 at 2.0 A resolution., Li M, Zhang PF, Pan XW, Chang WR, Biochem Biophys Res Commun. 2007 May 11;356(3):616-21. Epub 2007 Mar 12. PMID:17374362
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