1NSH
Solution Structure of Rabbit apo-S100A11 (19 models)
Summary for 1NSH
| Entry DOI | 10.2210/pdb1nsh/pdb |
| NMR Information | BMRB: 5189 |
| Descriptor | Calgizzarin (1 entity in total) |
| Functional Keywords | calcium-binding protein, ef hand, helix-loop-helix, s100, annexin, metal binding protein |
| Biological source | Oryctolagus cuniculus (rabbit) |
| Cellular location | Cytoplasm: P24480 |
| Total number of polymer chains | 2 |
| Total formula weight | 22625.88 |
| Authors | Dempsey, A.C.,Walsh, M.P.,Shaw, G.S. (deposition date: 2003-01-27, release date: 2003-07-15, Last modification date: 2024-05-22) |
| Primary citation | Dempsey, A.C.,Walsh, M.P.,Shaw, G.S. Unmasking the Annexin I Interaction from the structure of apo-S100A11 Structure, 11:887-897, 2003 Cited by PubMed Abstract: 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. PubMed: 12842051DOI: 10.1016/S0969-2126(03)00126-6 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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