Docking interactions in protein kinase and phosphatase networks

被引:145
作者
Remenyi, Attila [1 ]
Good, Matthew C. [1 ]
Lim, Wendell A. [1 ]
机构
[1] Univ Calif San Francisco, Program Biol Sci, Dept Mol & Cellular Pharmacol, San Francisco, CA 94143 USA
关键词
D O I
10.1016/j.sbi.2006.10.008
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
To achieve high biological specificity, protein kinases and phosphatases often recognize their targets through interactions that occur outside of the active site. Although the role of modular protein-protein interaction domains in kinase and phosphatase signaling has been well characterized, it is becoming clear that many kinases and phosphatases utilize docking interactions - recognition of a short peptide motif in target partners by a groove on the catalytic domain that is separate from the active site. Docking is particularly prevalent in serine/threonine kinases and phosphatases, and is a versatile organizational tool for building complex signaling networks; it confers a high degree of specificity and, in some cases, allosteric regulation.
引用
收藏
页码:676 / 685
页数:10
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