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Structural basis of calcium-induced E-cadherin rigidification and dimerization
1Department of Molecular and Medical Genetics, University of Toronto, Ontario, Canada.
Nature
|March 28, 1996
Summary
Epithelial cadherin (E-cadherin) structure reveals calcium ions rigidify and dimerize the molecule, crucial for cell adhesion and tissue formation. This finding clarifies cadherin function in maintaining solid tissues.
Area of Science:
- Molecular biology
- Structural biology
- Biochemistry
Background:
- Cadherins mediate cell adhesion and are vital for tissue development.
- Epithelial cadherin (E-cadherin) levels correlate with tumor invasiveness.
- Cadherin function is calcium-dependent, influencing conformation and stability.
Purpose of the Study:
- To elucidate the structural basis of E-cadherin function.
- To determine the role of calcium in E-cadherin conformation and dimerization.
- To provide insights into cadherin-mediated cell adhesion.
Main Methods:
- X-ray crystallography at 2.0 A resolution.
- Structural analysis of the two N-terminal extracellular domains of E-cadherin.
- Investigation of E-cadherin in the presence of calcium.
Main Results:
- The crystal structure reveals a two-fold symmetric dimer of E-cadherin N-terminal domains.
- Each E-cadherin molecule binds three bridged calcium ions.
- Calcium ions linearize, rigidify, and promote dimerization of E-cadherin.
Conclusions:
- The structure defines the role of calcium in stabilizing E-cadherin dimers.
- This provides a molecular understanding of cadherin-mediated cell adhesion.
- The findings are critical for understanding the maintenance of solid tissues.