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
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites
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Cadherins / chemistry*
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Cadherins / physiology*
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Calcium / physiology
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Cell Adhesion / physiology*
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Cloning, Molecular
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Crystallography, X-Ray
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Escherichia coli
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Mice
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Models, Molecular
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Molecular Sequence Data
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Protein Binding
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Protein Conformation
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Recombinant Fusion Proteins
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Structure-Activity Relationship
Substances
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Cadherins
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Recombinant Fusion Proteins
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Calcium