Structure of a calpain Ca2+-binding domain reveals a novel EF-hand and Ca2+-induced conformational changes

被引:179
作者
Blanchard, H
Grochulski, P
Li, Y
Arthur, JSC
Davies, PL
Elce, JS
Cygler, M
机构
[1] NATL RES COUNCIL CANADA, BIOTECHNOL RES INST, MONTREAL, PQ H4P 2R2, CANADA
[2] TECH UNIV LODZ, INST PHYS, PL-93005 LODZ, POLAND
[3] QUEENS UNIV, DEPT BIOCHEM, KINGSTON, ON K7L 3N6, CANADA
关键词
D O I
10.1038/nsb0797-532
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The crystal structure of a Ca2+-binding domain (dVI) of rat m-calpain has been determined at 2.3 Angstrom resolution, both with and without bound Ca2+. The structures reveal a unique fold incorporating five EF-hand motifs per monomer, three of which bind calcium at physiological calcium concentrations, with one showing a novel EF-hand coordination pattern. This investigation gives us a first view of the calcium-induced conformational changes, and consequently an insight into the mechanism of calcium induced activation in calpain. The crystal structures reveal a dVI homodimer which provides a preliminary model for the subunit dimerization in calpain.
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收藏
页码:532 / 538
页数:7
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