C-Cadherin Ectodomain Structure and Implications for Cell Adhesion Mechanisms

DOI Web Site 被引用文献34件
  • Titus J. Boggon
    Departments of Biochemistry and Molecular Biophysics,
  • John Murray
    Departments of Biochemistry and Molecular Biophysics,
  • Sophie Chappuis-Flament
    Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.
  • Ellen Wong
    Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.
  • Barry M. Gumbiner
    Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.
  • Lawrence Shapiro
    Departments of Biochemistry and Molecular Biophysics,

抄録

<jats:p>Cadherins are transmembrane proteins that mediate adhesion between cells in the solid tissues of animals. Here we present the 3.1 angstrom resolution crystal structure of the whole, functional extracellular domain from C-cadherin, a representative “classical” cadherin. The structure suggests a molecular mechanism for adhesion between cells by classical cadherins, and it provides a new framework for understanding both cis (same cell) and trans (juxtaposed cell) cadherin interactions. The trans adhesive interface is a twofold symmetric interaction defined by a conserved tryptophan side chain at the membrane-distal end of a cadherin molecule from one cell, which inserts into a hydrophobic pocket at the membrane-distal end of a cadherin molecule from the opposing cell.</jats:p>

収録刊行物

  • Science

    Science 296 (5571), 1308-1313, 2002-05-17

    American Association for the Advancement of Science (AAAS)

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