1A03

THE THREE-DIMENSIONAL STRUCTURE OF CA2+-BOUND CALCYCLIN: IMPLICATIONS FOR CA2+-SIGNAL TRANSDUCTION BY S100 PROTEINS, NMR, 20 STRUCTURES

1A03 の概要

• エントリーDOI: 10.2210/pdb1a03/pdb
• 分子名称: CALCYCLIN (RABBIT, CA2+) (1 entity in total)
• 機能のキーワード: calcium-binding protein, ef-hand, s-100 protein
• 由来する生物種: Oryctolagus cuniculus (rabbit)
• 細胞内の位置: Nucleus envelope (By similarity): P30801
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 20335.46

構造登録者

Sastry, M.,Ketchem, R.R.,Crescenzi, O.,Weber, C.,Lubienski, M.J.,Hidaka, H.,Chazin, W.J. (登録日: 1997-12-08, 公開日: 1999-03-02, 最終更新日: 2024-05-22)

主引用文献

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

実験手法

SOLUTION NMR