Structural basis of cell-cell adhesion by cadherins

Nature. 1995 Mar 23;374(6520):327-37. doi: 10.1038/374327a0.

Abstract

Crystal structures of the amino-terminal domain of N-cadherin provide a picture at the atomic level of a specific adhesive contact between cells. A repeated set of dimer interfaces is common to the structure in three lattices. These interactions combine to form a linear zipper of molecules that mirrors the linear structure of the intracellular filaments with which cadherins associate. This cell-adhesion zipper may provide a mechanism to marshal individual molecular adhesive interactions into strong bonds between cells.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cadherins / chemistry*
  • Cadherins / physiology*
  • Calcium / physiology
  • Cell Adhesion / physiology*
  • Cloning, Molecular
  • Crystallography, X-Ray
  • Escherichia coli
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Protein Conformation
  • Recombinant Fusion Proteins
  • Structure-Activity Relationship

Substances

  • Cadherins
  • Recombinant Fusion Proteins
  • Calcium