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1q1p

From Proteopedia

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{{STRUCTURE_1q1p| PDB=1q1p | SCENE= }}
{{STRUCTURE_1q1p| PDB=1q1p | SCENE= }}
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'''E-Cadherin activation'''
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===E-Cadherin activation===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15071499 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15071499}}
==About this Structure==
==About this Structure==
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[[Category: Stetefeld, J.]]
[[Category: Stetefeld, J.]]
[[Category: Cell-adhesion]]
[[Category: Cell-adhesion]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:45:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:01:45 2008''

Revision as of 12:01, 27 July 2008

Image:1q1p.png

Template:STRUCTURE 1q1p

E-Cadherin activation

Template:ABSTRACT PUBMED 15071499

About this Structure

1Q1P is a Single protein structure of sequence from Mus musculus. 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 Sun Jul 27 15:01:45 2008

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