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PMID: 7885471 Published · ppublish English Journal Article 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.

Structural basis of cell-cell adhesion by cadherins.

Nature ·Vol. 374 ·No. 6520 ·1995-03-23 ·Pages 327-37

Shapiro L, Fannon AM, Kwong PD, Thompson A, Lehmann MS, Grübel G, Legrand JF, Als-Nielsen J, Colman DR, Hendrickson WA

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.

MeSH Terms
Amino Acid Sequence Animals Binding Sites Cadherins/chemistry,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
Chemicals
Cadherins Recombinant Fusion Proteins Calcium
Authors & Affiliations
10 authors, click to expand affiliations / ORCID
Shapiro L
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032.
Fannon A M
Kwong P D
Thompson A
Lehmann M S
Grübel G
Legrand J F
Als-Nielsen J
Colman D R
Hendrickson W A
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1995-03-23
Pages
327-37
Language
English
Region
England
NLM ID
0410462
Subset
IM
Corrections
CommentIn
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