1A03
THE THREE-DIMENSIONAL STRUCTURE OF CA2+-BOUND CALCYCLIN: IMPLICATIONS FOR CA2+-SIGNAL TRANSDUCTION BY S100 PROTEINS, NMR, 20 STRUCTURES
Summary for 1A03
Entry DOI | 10.2210/pdb1a03/pdb |
Descriptor | CALCYCLIN (RABBIT, CA2+) (1 entity in total) |
Functional Keywords | calcium-binding protein, ef-hand, 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 | Sastry, M.,Ketchem, R.R.,Crescenzi, O.,Weber, C.,Lubienski, M.J.,Hidaka, H.,Chazin, W.J. (deposition date: 1997-12-08, release date: 1999-03-02, Last modification date: 2024-05-22) |
Primary citation | Sastry, M.,Ketchem, R.R.,Crescenzi, O.,Weber, C.,Lubienski, M.J.,Hidaka, H.,Chazin, W.J. The three-dimensional structure of Ca(2+)-bound calcyclin: implications for Ca(2+)-signal transduction by S100 proteins. Structure, 6:223-231, 1998 Cited by PubMed Abstract: Calcyclin is a member of the S100 subfamily of EF-hand Ca(2+)-binding proteins. This protein has implied roles in the regulation of cell growth and division, exhibits deregulated expression in association with cell transformation, and is found in high abundance in certain breast cancer cell lines. The novel homodimeric structural motif first identified for apo calcyclin raised the possibility that S100 proteins recognize their targets in a manner that is distinctly different from that of the prototypical EF-hand Ca2+ sensor, calmodulin. The NMR solution structure of Ca(2+)-bound calcyclin has been determined in order to identify Ca(2+)-induced structural changes and to obtain insights into the mechanism of Ca(2+)-triggered target protein recognition. PubMed: 9519412DOI: 10.1016/S0969-2126(98)00023-9 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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