1q1p
From Proteopedia
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(New page: 200px<br /><applet load="1q1p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q1p, resolution 3.20Å" /> '''E-Cadherin activatio...)
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Revision as of 22:11, 20 November 2007
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E-Cadherin activation
Overview
Cellular adhesion by classical cadherins depends critically on the exact, proteolytic removal of their N-terminal prosequences. In this combined, solution NMR and X-ray crystallographic study, the consequences of, propeptide cleavage of an epithelial cadherin construct (domains 1 and 2), were followed at atomic level. At low protein concentration, the, N-terminal processing induces docking of the tryptophan-2 side-chain into, a binding pocket on the same molecule. At high concentration, cleavage, induces dimerization (KD=0.72 mM, k(off)=0.7 s(-1)) and concomitant, intermolecular exchange of the betaA-strands and the tryptophan-2, side-chains. Thus, the cleavage represents the switch from a nonadhesive, to the functional form of cadherin.
About this Structure
1Q1P is a Single protein structure of sequence from Mus musculus with CA as ligand. Full crystallographic information is available from OCA.
Reference
Proteolytic E-cadherin activation followed by solution NMR and X-ray crystallography., Haussinger D, Ahrens T, Aberle T, Engel J, Stetefeld J, Grzesiek S, EMBO J. 2004 Apr 21;23(8):1699-708. Epub 2004 Apr 8. PMID:15071499
Page seeded by OCA on Wed Nov 21 00:18:36 2007
