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

Helen Blanchard, Pawel Grochulski, Yunge Li, J. Simon C. Arthur, Peter L. Davies, John S. Elce, Miroslaw Cygler (Lead / Corresponding author)

Research output: Contribution to journalArticlepeer-review

186 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)532-538
Number of pages7
JournalNature Structural Biology
Volume4
Issue number7
DOIs
Publication statusPublished - 1 Jul 1997

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

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