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Primary citation
Title Structural Basis of the Ca2+ Dependent Association between S100C (S100A11) and its Target, the N-Terminal Part of Annexin I
Authors Rety, S.search; Osterloh, D.search; Arie, J.P.search; Tabaries, S.search; Seeman, J.search; Russo-Marie, F.search; Gerke, V.search; Lewit-Bentley, A.search
Journal STRUCTUREsearch vol:8, pag:175 (2000), Identifiers: PubMed ID (10673436)search DOI (10.1016/S0969-2126(00)00093-9)
Abstract S100C (S100A11) is a member of the S100 calcium-binding protein family, the function of which is not yet entirely clear, but may include cytoskeleton assembly and dynamics. S100 proteins consist of two EF-hand calcium-binding motifs, connected by a flexible loop. Like several other members of the family, S100C forms a homodimer. A number of S100 proteins form complexes with annexins, another family of calcium-binding proteins that also bind to phospholipids. Structural studies have been undertaken to understand the basis of these interactions.
MeSH terms Acetylationsearch, Annexin A1search, Calciumsearch, Crystallographysearch, X-Raysearch, Disulfidessearch, Modelssearch, Molecularsearch, Protein Conformationsearch, Recombinant Proteinssearch, S100 Proteinssearch, Spectrometrysearch, Fluorescencesearch
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