1nsh | pdb_00001nsh

Solution Structure of Rabbit apo-S100A11 (19 models)

spinqualitylabelsall models 1nsh, 19 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1nsh is a 2 chain structure with sequence from Oryctolagus cuniculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: S100A11 OR S100C OR PCALG (Oryctolagus cuniculus) 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 S100A11 is a homodimeric EF-hand calcium binding protein that undergoes a calcium-induced conformational change and interacts with the phospholipid binding protein annexin I to coordinate membrane association. In this work, the solution structure of apo-S100A11 has been determined by NMR spectroscopy to uncover the details of its calcium-induced structural change. Apo-S100A11 forms a tight globular structure having a near antiparallel orientation of helices III and IV in calcium binding site II. Further, helices I and IV, and I and I', form a more closed arrangement than observed in other apo-S100 proteins. This helix arrangement in apo-S100A11 partially buries residues in helices I (P3, E11, A15), III (V55, R58, M59), and IV (A86, C87, S90) and the linker (A45, F46), which are required for interaction with annexin I in the calcium-bound state. In apo-S100A11, this results in a "masked" binding surface that prevents annexin I binding but is uncovered upon calcium binding. Unmasking the annexin I interaction from the structure of Apo-S100A11.,Dempsey AC, Walsh MP, Shaw GS Structure. 2003 Jul;11(7):887-97. PMID:12842051 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also S100 protein

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