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

+ See all authors and affiliations

Science  02 Jan 1998:
Vol. 279, Issue 5347, pp. 88-91
DOI: 10.1126/science.279.5347.88

You are currently viewing the abstract.

View Full Text

Via your Institution

Log in through your institution

Log in through your institution


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.

  • * To whom correspondence should be addressed. E-mail: aweiss{at}

View Full Text

Related Content