Dimerization-Induced Inhibition of Receptor Protein Tyrosine Phosphatase Function Through an Inhibitory Wedge-Reference-Cited by-同舟云学术

Dimerization-Induced Inhibition of Receptor Protein Tyrosine Phosphatase Function Through an Inhibitory Wedge

Published:1998-01-02 Issue:5347 Volume:279 Page:88-91
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Majeti Ravindra¹²³,Bilwes Alexandrine M.¹²³,Noel Joseph P.¹²³,Hunter Tony¹²³,Weiss Arthur¹²³

Affiliation:

1. R. Majeti and A. Weiss, Biomedical Sciences Graduate Program, Departments of Microbiology and Immunology and of Medicine and the Howard Hughes Medical Institute, University of California, San Francisco, CA 94143, USA.

2. A. M. Bilwes and J. P. Noel, Structural Biology Laboratory, The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, CA 92037, USA.

3. T. Hunter, Molecular Biology and Virology Laboratory, The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, CA 92037, USA.

Abstract

The function and regulation of the receptorlike transmembrane protein tyrosine phosphatases (RPTPs) are not well understood. Ligand-induced dimerization inhibited the function of the epidermal growth factor receptor (EGFR)–RPTP CD45 chimera (EGFR-CD45) in T cell signal transduction. Properties of mutated EGFR-CD45 chimeras supported a general model for the regulation of RPTPs, derived from the crystal structure of the RPTPα membrane-proximal phosphatase domain. The phosphatase domain apparently forms a symmetrical dimer in which the catalytic site of one molecule is blocked by specific contacts with a wedge from the other.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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