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Originally published in Science Express on 18 April 2002
Science 17 May 2002:
Vol. 296. no. 5571, pp. 1308 - 1313
DOI: 10.1126/science.1071559

Reports

C-Cadherin Ectodomain Structure and Implications for Cell Adhesion Mechanisms

Titus J. Boggon,14 John Murray,14 Sophie Chappuis-Flament,5 Ellen Wong,5 Barry M. Gumbiner,5 Lawrence Shapiro1234*

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.

1 Departments of Biochemistry and Molecular Biophysics,
2 Department of Ophthalmology,
3 Naomi Berrie Diabetes Center, Columbia University College of Physicians and Surgeons, 630 West 168th Street, New York, NY 10032, USA.
4 Structural Biology Program, Department of Physiology and Biophysics, Mount Sinai School of Medicine, New York, NY 10029, USA.
5 Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.
*   To whom correspondence should be addressed. E-mail: Shapiro{at}convex.hhmi.columbia.edu


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