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Journal article

Structure of a tyrosine phosphatase adhesive interaction reveals a spacer-clamp mechanism.

Abstract:

Cell-cell contacts are fundamental to multicellular organisms and are subject to exquisite levels of control. Human RPTPmu is a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes. Here we describe a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching t...

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Publication status:
Published

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Publisher copy:
10.1126/science.1144646

Authors


More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Biology
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Biology
Role:
Author
Journal:
Science (New York, N.Y.) More from this journal
Volume:
317
Issue:
5842
Pages:
1217-1220
Publication date:
2007-08-01
DOI:
EISSN:
1095-9203
ISSN:
0036-8075

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