Dimerization-induced inhibition of receptor protein tyrosine phosphatase function through an inhibitory wedge

被引：214

作者：

Majeti, R

Bilwes, AM

Noel, JP

Hunter, T

Weiss, A ^{[1
]}

机构：

[1] Univ Calif San Francisco, Dept Microbiol & Immunol, Biomed Sci Grad Program, San Francisco, CA 94143 USA

[2] Univ Calif San Francisco, Dept Med, Biomed Sci Grad Program, San Francisco, CA 94143 USA

[3] Univ Calif San Francisco, Howard Hughes Med Inst, San Francisco, CA 94143 USA

[4] Salk Inst Biol Studies, Struct Biol Lab, La Jolla, CA 92037 USA

[5] Salk Inst Biol Studies, Mol Biol & Virol Lab, La Jolla, CA 92037 USA

来源：

SCIENCE | 1998年 / 279卷 / 5347期

关键词：

D O I：

10.1126/science.279.5347.88

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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 RPTP alpha 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.

引用

页码：88 / 91

页数：4

共 23 条

[1] Structural basis for inhibition of receptor protein-tyrosine phosphatase-alpha by dimerization [J].