Structures of Src-family tyrosine kinases

被引:324
作者
Sicheri, F [1 ]
Kuriyan, J [1 ]
机构
[1] Rockefeller Univ, Howard Hughes Med Inst, Mol Biophys Lab, New York, NY 10021 USA
关键词
D O I
10.1016/S0959-440X(97)80146-7
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 structures of three Src-family tyrosine kinases have been determined recently. The structure of the catalytic domain of Lck has been determined in the active autophosphorylated state. The structures of larger constructs of c-Src and Hck, containing the SH3, SH2 and catalytic domains, as well as a C-terminal regulatory tail, have been determined in the down-regulated stale, phosphorylated in the C-terminal tail. A comparison of these structures leads to an unanticipated mechanism for the regulation of catalytic activity by cooperative interactions between the SH2, SH3 and catalytic domains. (C) Current Biology Ltd ISSN 0959-440X.
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收藏
页码:777 / 785
页数:9
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