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Docking interactions in protein kinase and phosphatase networks
被引:145
作者:

Remenyi, Attila
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机构:
Univ Calif San Francisco, Program Biol Sci, Dept Mol & Cellular Pharmacol, San Francisco, CA 94143 USA Univ Calif San Francisco, Program Biol Sci, Dept Mol & Cellular Pharmacol, San Francisco, CA 94143 USA

Good, Matthew C.
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机构:
Univ Calif San Francisco, Program Biol Sci, Dept Mol & Cellular Pharmacol, San Francisco, CA 94143 USA Univ Calif San Francisco, Program Biol Sci, Dept Mol & Cellular Pharmacol, San Francisco, CA 94143 USA

Lim, Wendell A.
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h-index: 0
机构:
Univ Calif San Francisco, Program Biol Sci, Dept Mol & Cellular Pharmacol, San Francisco, CA 94143 USA Univ Calif San Francisco, Program Biol Sci, Dept Mol & Cellular Pharmacol, San Francisco, CA 94143 USA
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.
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页码:676 / 685
页数:10
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