1CNP
THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD FOR S100 CA2+-BINDING PROTEINS, NMR, 22 STRUCTURES
Summary for 1CNP
| Entry DOI | 10.2210/pdb1cnp/pdb |
| Descriptor | CALCYCLIN (RABBIT, APO) (1 entity in total) |
| Functional Keywords | ef-hand, calcium-binding protein, s-100 protein |
| Biological source | Oryctolagus cuniculus (rabbit) |
| Cellular location | Nucleus envelope (By similarity): P30801 |
| Total number of polymer chains | 2 |
| Total formula weight | 20335.46 |
| Authors | Potts, B.C.M.,Smith, J.,Akke, M.,Macke, T.J.,Okazaki, K.,Hidaka, H.,Case, D.A.,Chazin, W.J. (deposition date: 1995-08-31, release date: 1996-10-14, Last modification date: 2024-05-22) |
| Primary citation | Potts, B.C.,Smith, J.,Akke, M.,Macke, T.J.,Okazaki, K.,Hidaka, H.,Case, D.A.,Chazin, W.J. The structure of calcyclin reveals a novel homodimeric fold for S100 Ca(2+)-binding proteins. Nat.Struct.Biol., 2:790-796, 1995 Cited by PubMed Abstract: The S100 calcium-binding proteins are implicated as effectors in calcium-mediated signal transduction pathways. The three-dimensional structure of the S100 protein calcyclin has been determined in solution in the apo state by NMR spectroscopy and a computational strategy that incorporates a systematic docking protocol. This structure reveals a symmetric homodimeric fold that is unique among calcium-binding proteins. Dimerization is mediated by hydrophobic contacts from several highly conserved residues, which suggests that the dimer fold identified for calcyclin will serve as a structural paradigm for the S100 subfamily of calcium-binding proteins. PubMed: 7552751DOI: 10.1038/nsb0995-790 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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