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Curr Opin Struct Biol. 2006 Dec;16(6):676-85. Epub 2006 Oct 31.

Docking interactions in protein kinase and phosphatase networks.

Author information

1
Department of Cellular and Molecular Pharmacology, Program in Biological Sciences, University of California San Francisco, 600 16th Street, San Francisco, CA 94143-2240, USA.

Abstract

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.

PMID:
17079133
DOI:
10.1016/j.sbi.2006.10.008
[Indexed for MEDLINE]

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