1l3w
From Proteopedia
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C-cadherin Ectodomain
Overview
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.
About this Structure
1L3W is a Single protein structure of sequence from Xenopus laevis with NAG, NDG and CA as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Tue Nov 20 20:13:56 2007
Categories: Single protein | Xenopus laevis | Boggon, T.J. | Chappuis-Flament, S. | Gumbiner, B.M. | Murray, J. | Shapiro, L. | Wong, E. | CA | NAG | NDG | Cadherin | Calcium binding | Cell adhesion | Ectodomain | Extracellular
