Revealing mechanisms for SH2 domain mediated regulation of the protein tyrosine phosphatase SHP-2

被引：260
作者：
Barford, D
Neel, BG
机构：
[1] Univ Oxford, Mol Biophys Lab, Oxford OX1 3QU, England
[2] Harvard Univ, Sch Med, Beth Israel Deaconess Med Ctr, Dept Med,Div Hematol & Oncol, Boston, MA 02215 USA
来源：
STRUCTURE | 1998年 / 6卷 / 03期
关键词：
D O I：
10.1016/S0969-2126(98)00027-6
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The crystal structure of the protein tyrosine phosphatase SHP-2 reveals the mechanism of auto-inhibition of phosphatase activity by its SH2 domains, Phosphotyrosine peptide stimulation of the phosphatase activity, resulting from peptide binding to the N-terminal SH2 domain, is linked to conformational changes within the protein, including an unprecedented allosteric transition of the N-terminal SH2 domain.
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页码：249 / 254
页数：6
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