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Structural basis of cell-cell adhesion by cadherins

Nature volume 374, pages 327–337 (1995)Cite this article

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.

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Author information

Author notes

  1. Jean-François Legrand

    Present address: Laboratoire de Spectrometrie Physique (URA CNRS no. 8), Universite J. Fourier-Grenoble 1, BP87, 38402, Saint Martin d'Heres Cedex, France

  2. Jens Als-Nielsen

    Present address: Ris0 National Laboratory, DK 4000, Roskilde, Denmark

Authors and Affiliations

  1. Department of Biochemistry and Molecular Biophysics, and,

    Lawrence Shapiro, Peter D. Kwong & Wayne A. Hendrickson

  2. Howard Hughes Medical Institute, Columbia University, New York, New York, 10032, USA

    Wayne A. Hendrickson

  3. Brookdale Center for Molecular Biology, Mount Sinai School of Medicine, New York, New York, 10029, USA

    Allison M. Fannon & David R. Colman

  4. European Molecular Biology Laboratory, BP 156 X, 38042, Grenoble, France

    Andrew Thompson

  5. European Synchrotron Radiation Facility, BP 220, 38043, Grenoble, France

    Mogens S. Lehmann, Gerhard Grübel, Jean-François Legrand & Jens Als-Nielsen

  6. Institut Laue Langevin, BP 156 X, 38042, Grenoble, France

    Mogens S. Lehmann

  7. Laboratoire de Spectrometrie Physique (URA CNRS no. 8), Universite J. Fourier-Grenoble 1, BP87, 38402, Saint Martin d'Heres Cedex, France

    Jens Als-Nielsen

Authors
  1. Lawrence Shapiro
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Shapiro, L., Fannon, A., Kwong, P. et al. Structural basis of cell-cell adhesion by cadherins. Nature 374, 327–337 (1995). https://doi.org/10.1038/374327a0

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