Publication Abstract from PubMed
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.
C-cadherin ectodomain structure and implications for cell adhesion mechanisms.,Boggon TJ, Murray J, Chappuis-Flament S, Wong E, Gumbiner BM, Shapiro L Science. 2002 May 17;296(5571):1308-13. Epub 2002 Apr 18. PMID:11964443[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
