1ff5

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(New page: 200px<br /><applet load="1ff5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ff5, resolution 2.93&Aring;" /> '''STRUCTURE OF E-CADHE...)
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Revision as of 12:45, 20 November 2007

Image:1ff5.gif

1ff5, resolution 2.93Å

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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, (>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.

About this Structure

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

Reference

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

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