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

TY - JOUR

T1 - Structure of a calpain Ca2+-binding domain reveals a novel EF-hand and Ca2+-induced conformational changes

AU - Blanchard, Helen

AU - Grochulski, Pawel

AU - Li, Yunge

AU - Arthur, J. Simon C.

AU - Davies, Peter L.

AU - Elce, John S.

AU - Cygler, Miroslaw

PY - 1997/7/1

Y1 - 1997/7/1

N2 - The crystal structure of a Ca2+-binding domain (dVI) of rat m-calpain has been determined at 2.3 Å 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.

AB - The crystal structure of a Ca2+-binding domain (dVI) of rat m-calpain has been determined at 2.3 Å 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.

UR - https://www.scopus.com/pages/publications/0030998285

U2 - 10.1038/nsb0797-532

DO - 10.1038/nsb0797-532

M3 - Article

C2 - 9228945

AN - SCOPUS:0030998285

SN - 1072-8368

VL - 4

SP - 532

EP - 538

JO - Nature Structural Biology

JF - Nature Structural Biology

IS - 7

ER -