C1, see them all

被引:17
作者
Hall, C
Lim, L
Leung, T
机构
[1] UCL, Inst Neurol, Dept Mol Neurosci, London WC1N 1PJ, England
[2] GSK IMCB Grp, Inst Mol & Cell Biol, Singapore 138673, Singapore
关键词
D O I
10.1016/j.tibs.2005.02.003
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
Recent structural analysis of crystalline beta 2-chimaerin shows the central protein kinase C-like, diacyclglycerol (DAG)-binding C1 domain to be masked by its intramolecular interactions with the N-terminal SH2 and GAP domains, and linker regions. A mechanism of activation has been derived from modelling of a GAP-Rac GTPase complex - the auto-inhibitory constraints are released via membrane engagement, unmasking the C1 domain to enable DAG binding and subsequent GAP stimulation of Rac GTPase catalytic activity.
引用
收藏
页码:169 / 171
页数:3
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