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Updated: Jul 9, 2026
13:22
Adhesion Frequency Assay for In Situ Kinetics Analysis of Cross-Junctional Molecular Interactions at the Cell-Cell Interface
Published on: November 2, 2011
C-cadherin ectodomain structure and implications for cell adhesion mechanisms.
Titus J Boggon1, John Murray, Sophie Chappuis-Flament
1Department of Biochemistry, Columbia University College of Physicians and Surgeons, 630 West 168th Street, New York, NY 10032, USA.
Science (New York, N.Y.)
|April 20, 2002
Summary
The crystal structure of C-cadherin reveals how these cell adhesion proteins bind. This finding provides a new framework for understanding cadherin interactions in animal tissues.
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- Cadherins are crucial transmembrane proteins responsible for cell-cell adhesion in animal tissues.
- Understanding cadherin function is vital for comprehending tissue development and integrity.
Purpose of the Study:
- To determine the high-resolution crystal structure of the extracellular domain of C-cadherin.
- To elucidate the molecular mechanisms underlying classical cadherin-mediated cell adhesion.
Main Methods:
- X-ray crystallography was employed to obtain the 3.1 angstrom resolution structure.
- The study focused on the entire functional extracellular domain of C-cadherin.
Main Results:
- The crystal structure of the C-cadherin extracellular domain was determined at 3.1 angstrom resolution.
- A molecular mechanism for trans-cadherin adhesion was proposed, involving a conserved tryptophan.
- The structure offers insights into both cis and trans cadherin interactions.
Conclusions:
- The determined structure provides a molecular basis for classical cadherin-mediated cell adhesion.
- This work establishes a new framework for studying cadherin interactions at the cellular level.
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