1aj5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search

OCA (Talk | contribs)
(New page: 200px<br /><applet load="1aj5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aj5, resolution 2.30&Aring;" /> '''CALPAIN DOMAIN VI AP...)
Next diff →

Revision as of 08:46, 20 November 2007


1aj5, resolution 2.30Å

Drag the structure with the mouse to rotate

CALPAIN DOMAIN VI APO

Overview

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.

About this Structure

1AJ5 is a Single protein structure of sequence from Rattus norvegicus. Active as Hydrolase, with EC number and 3.4.22.53 3.4.22.52 and 3.4.22.53 Full crystallographic information is available from OCA.

Reference

Structure of a calpain Ca(2+)-binding domain reveals a novel EF-hand and Ca(2+)-induced conformational changes., Blanchard H, Grochulski P, Li Y, Arthur JS, Davies PL, Elce JS, Cygler M, Nat Struct Biol. 1997 Jul;4(7):532-8. PMID:9228945

Page seeded by OCA on Tue Nov 20 10:53:51 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools