1ff5: Difference between revisions

Revision as of 03:09, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ff5.png

Template:STRUCTURE 1ff5

STRUCTURE OF E-CADHERIN DOUBLE DOMAINSTRUCTURE OF E-CADHERIN DOUBLE DOMAIN

Template:ABSTRACT PUBMED 10202138

About this StructureAbout this Structure

1FF5 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

A new crystal structure, Ca2+ dependence and mutational analysis reveal molecular details of E-cadherin homoassociation., Pertz O, Bozic D, Koch AW, Fauser C, Brancaccio A, Engel J, EMBO J. 1999 Apr 1;18(7):1738-47. PMID:10202138

Page seeded by OCA on Tue Jul 1 03:09:16 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1ff5.gif|left|200px]]
+{{Seed}}
+[[Image:1ff5.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1ff5|  PDB=1ff5  |  SCENE=  }}
-'''STRUCTURE OF E-CADHERIN DOUBLE DOMAIN'''
+===STRUCTURE OF E-CADHERIN DOUBLE DOMAIN===
-==Overview==
+<!--
-Electron microscopy of ECADCOMP, a recombinant E-cadherin ectodomain pentamerized by the assembly domain of cartilage oligomeric matrix protein, has been used to analyze the role of cis-dimerization and trans-interaction in the homophilic association of this cell adhesion molecule. The Ca2+ dependency of both interactions was investigated. Low Ca2+ concentrations (50 microM) stabilized the rod-like structure of E-cadherin. At medium Ca2+ concentration (500 microM), two adjacent ectodomains in a pentamer formed cis-dimers. At high Ca2+ concentration (&gt;1 mM), two cis-dimers from different pentamers formed a trans-interaction. The X-ray structure of an N-terminal domain pair of E-cadherin revealed two molecules per asymmetric unit in an intertwisted X-shaped arrangement with closest contacts in the Ca2+-binding region between domains 1 and 2. Contrary to previous data, Trp2 was docked in the hydrophobic cavity of its own molecule, and was therefore not involved in cis-dimerization of two molecules. This was supported further by W2A and A80I (a residue involved in the hydrophobic cavity surrounding Trp2) mutations in ECADCOMP which both led to abrogation of the trans- but not the cis-interaction. Structural and biochemical data suggest a link between Ca2+ binding in the millimolar range and Trp2 docking, both events being essential for the trans-association.
+The line below this paragraph, {{ABSTRACT_PUBMED_10202138}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10202138 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10202138}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Ca-binding]]
 [[Category: E-cadherin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:15:10 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 03:09:16 2008''