1DVI

CALPAIN DOMAIN VI WITH CALCIUM BOUND

Summary for 1DVI

• Entry DOI: 10.2210/pdb1dvi/pdb
• Descriptor: CALPAIN, CALCIUM ION (3 entities in total)
• Functional Keywords: calcium-dependent protease, small subunit
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cytoplasm: Q64537
• Total number of polymer chains: 2
• Total formula weight: 42898.45

Authors

Cygler, M.,Blanchard, H.,Grochulski, P. (deposition date: 1997-05-15, release date: 1998-05-27, Last modification date: 2024-02-07)

Primary citation

Blanchard, H.,Grochulski, P.,Li, Y.,Arthur, J.S.,Davies, P.L.,Elce, J.S.,Cygler, M.
Structure of a calpain Ca(2+)-binding domain reveals a novel EF-hand and Ca(2+)-induced conformational changes.
Nat.Struct.Biol., 4:532-538, 1997

PubMed Abstract: The crystal structure of a Ca(2+)-binding domain (dVI) of rat m-calpain has been determined at 2.3 A 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.

PubMed: 9228945
DOI: 10.1038/nsb0797-532

Experimental method

X-RAY DIFFRACTION (2.3 Å)