Revealing mechanisms for SH2 domain mediated regulation of the protein tyrosine phosphatase SHP-2
Revealing mechanisms for SH2 domain mediated regulation of the protein tyrosine phosphatase SHP-2
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DOI：
10.1016/s0969-2126(98)00027-6
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发表时间：
1998-03-15
期刊：
影响因子：
5.7
通讯作者：
Neel, BG
中科院分区：
文献类型：
--
作者：
Barford, D;Neel, BG
蛋白酪氨酸磷酸酶SHP-2的晶体结构揭示了其SH 2结构域对磷酸酶活性的自抑制机制。磷酸酪氨酸肽对磷酸酶活性的刺激（由肽与N-末端SH 2结构域结合引起）与蛋白质内的构象变化有关，包括N-末端SH 2结构域的前所未有的变构转变。
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.