1CFP
S100B (S100BETA) NMR DATA WAS COLLECTED FROM A SAMPLE OF CALCIUM FREE PROTEIN AT PH 6.3 AND A TEMPERATURE OF 311 K AND 1.7-6.9 MM CONCENTRATION, 25 STRUCTURES
Summary for 1CFP
Entry DOI | 10.2210/pdb1cfp/pdb |
Descriptor | S100B (1 entity in total) |
Functional Keywords | helix-loop-helix, calcium-binding protein |
Biological source | Bos taurus (cattle) |
Cellular location | Cytoplasm: P02638 |
Total number of polymer chains | 2 |
Total formula weight | 21363.95 |
Authors | Kilby, P.M.,Vaneldik, L.J.,Roberts, G.C.K. (deposition date: 1996-06-04, release date: 1997-03-12, Last modification date: 2024-05-22) |
Primary citation | Kilby, P.M.,Van Eldik, L.J.,Roberts, G.C. The solution structure of the bovine S100B protein dimer in the calcium-free state. Structure, 4:1041-1052, 1996 Cited by PubMed Abstract: S100B (S100beta) is a member of the S100 family of small calcium-binding proteins: members of this family contain two helix-loop-helix calcium-binding motifs and interact with a wide range of proteins involved mainly in the cytoskeleton and cell proliferation. S100B is a neurite-extension factor and levels of S100B are elevated in the brains of patients with Alzheimer's disease or Down's syndrome: the pattern of S100B overexpression in Alzheimer's disease correlates with the pattern of neuritic-plaque formation. Identification of a growing class of S100 proteins and the likely neurochemical importance of S100B make the determination of the structure of S100B of interest. PubMed: 8805590DOI: 10.1016/S0969-2126(96)00111-6 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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