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Structural basis of cell-cell adhesion by cadherins
L Shapiro1, A M Fannon, P D Kwong
1Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032.
Nature
|March 23, 1995
Summary
Crystal structures reveal how N-cadherin forms a molecular zipper, linking cells. This zipper mechanism strengthens cell adhesion by organizing individual interactions into robust bonds.
Area of Science:
- Structural biology
- Cell biology
- Biochemistry
Background:
- Cadherins are crucial for cell-cell adhesion.
- Understanding cadherin interactions at the atomic level is key to deciphering cell adhesion mechanisms.
Purpose of the Study:
- To elucidate the atomic-level structure of the N-cadherin amino-terminal domain.
- To understand the molecular basis of cadherin-mediated cell adhesion.
Main Methods:
- X-ray crystallography to determine crystal structures.
- Analysis of molecular interfaces and lattice formations.
Main Results:
- The amino-terminal domain of N-cadherin forms a linear zipper structure.
- A conserved set of dimer interfaces drives the zipper formation across different crystal lattices.
- This zipper structure mirrors the organization of intracellular filaments.
Conclusions:
- The N-cadherin zipper provides a structural mechanism for strong cell-cell adhesion.
- This mechanism may translate individual molecular interactions into collective, robust bonds.