C-cadherin ectodomain structure and implications for cell adhesion mechanisms Journal Article


Authors: Boggon, T. J.; Murray, J.; Chappuis-Flament, S.; Wong, E.; Gumbiner, B. M.; Shapiro, L.
Article Title: C-cadherin ectodomain structure and implications for cell adhesion mechanisms
Abstract: Cadherins are transmembrane proteins that mediate adhesion between cells in the solid tissues of animals. Here we present the 3.1 angstrom resolution crystal structure of the whole, functional extracellular domain from C-cadherin, a representative "classical" cadherin. The structure suggests a molecular mechanism for adhesion between cells by classical cadherins, and it provides a new framework for understanding both cis (same cell) and trans (juxtaposed cell) cadherin interactions. The trans adhesive interface is a twofold symmetric interaction defined by a conserved tryptophan side chain at the membrane-distal end of a cadherin molecule from one cell, which inserts into a hydrophobic pocket at the membrane-distal end of a cadherin molecule from the opposing cell.
Keywords: uvomorulin; dimerization; superfamily; complex; extracellular domain; junctions; homoassociation; calcium-binding
Journal Title: Science
Volume: 296
Issue: 5571
ISSN: 0036-8075
Publisher: American Association for the Advancement of Science  
Date Published: 2002-05-17
Start Page: 1308
End Page: 1313
Language: English
ACCESSION: WOS:000175713000052
DOI: 10.1126/science.1071559
PROVIDER: wos
PUBMED: 11964443
Notes: Article -- Source: Wos
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  1. Ellen   Wong
    14 Wong