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

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: 9519412
DOI: 10.1016/S0969-2126(98)00023-9

Experimental method

SOLUTION NMR