1UWO
CALCIUM FORM OF HUMAN S100B, NMR, 20 STRUCTURES
Summary for 1UWO
| Entry DOI | 10.2210/pdb1uwo/pdb |
| NMR Information | BMRB: 5206,5377 |
| Descriptor | S100B (1 entity in total) |
| Functional Keywords | human s100b, calcium-binding protein, ef-hand, conformational change, solution structure |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: P04271 |
| Total number of polymer chains | 2 |
| Total formula weight | 21191.68 |
| Authors | Smith, S.P.,Shaw, G.S. (deposition date: 1997-12-05, release date: 1998-06-10, Last modification date: 2024-05-22) |
| Primary citation | Smith, S.P.,Shaw, G.S. A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form. Structure, 6:211-222, 1998 Cited by PubMed Abstract: S100B is a homodimeric member of the EF-hand calcium-binding protein superfamily. The protein has been implicated in cellular processes such as cell differentiation and growth, plays a role in cytoskeletal structure and function, and may have a role in neuropathological diseases, such as Alzheimers. The effects of S100B are mediated via its interaction with target proteins. While several studies have suggested that this interaction is propagated through a calcium-induced conformational change, leading to the exposure of a hydrophobic region of S100B, the molecular details behind this structural alteration remain unclear. PubMed: 9519411DOI: 10.1016/S0969-2126(98)00022-7 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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