The conformational plasticity of protein kinases

被引：1379

作者：

Huse, M

Kuriyan, J ^{[1
]}

机构：

[1] Univ Calif Berkeley, Howard Hughes Med Inst, Dept Chem, Dept Mol & Cell Biol, Berkeley, CA 94720 USA

[2] Stanford Univ, Dept Biol Sci, Palo Alto, CA 94305 USA

[3] Univ Calif Berkeley, Lawrence Berkeley Lab, Phys Biosci Div, Berkeley, CA 94720 USA

来源：

CELL | 2002年 / 109卷 / 03期

关键词：

D O I：

10.1016/S0092-8674(02)00741-9

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：

Protein kinases operate in a large number of distinct signaling pathways, where the tight regulation of their catalytic activity is crucial to the development and maintenance of eukaryotic organisms. The catalytic domains of different kinases adopt strikingly similar structures when they are active. By contrast, crystal structures of inactive kinases have revealed a remarkable plasticity in the kinase domain that allows the adoption of distinct conformations in response to interactions with specific regulatory domains or proteins.

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页码：275 / 282

页数：8

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