The structure of the C-cadherin ectodomain resolved.

Structure (London, England : 1993) ·Vol. 10 ·No. 6 ·2002-06-00 ·Pages 739-40

Leckband D

Abstract

In a recent issue of Science, Boggon et al. report the structure of the full-length C-cadherin ectodomain (CCAD1-5). Previous cell adhesion and direct force measurements demonstrated that the CCAD1-5 ectodomain is a functionally active adhesion molecule, and thus the determination of its structure is a significant achievement.

MeSH Terms

Cadherins/chemistry,metabolism Cell Adhesion Molecules/chemistry,metabolism Protein Binding/physiology Protein Conformation Protein Structure, Tertiary Xenopus Proteins

Chemicals

CDH3 protein, Xenopus Cadherins Cell Adhesion Molecules Xenopus Proteins

Authors & Affiliations

1 authors, click to expand affiliations / ORCID

Leckband Deborah

Department of Chemical and Biomolecular Engineering and, Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA.

Article Info

Journal

Structure (London, England : 1993)

Abbr.

Structure

ISSN

0969-2126

DOI

10.1016/s0969-2126(02)00783-9

Published

2002-06-00

Pages

739-40

Language

English

Region

United States

NLM ID

101087697

Subset

External Links

PubMed source DOI: 10.1016/s0969-2126(02)00783-9 View journal details

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The structure of the C-cadherin ectodomain resolved.

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