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Review
. 2006 Dec;16(6):676-85.
doi: 10.1016/j.sbi.2006.10.008. Epub 2006 Oct 31.

Docking Interactions in Protein Kinase and Phosphatase Networks

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Review

Docking Interactions in Protein Kinase and Phosphatase Networks

Attila Reményi et al. Curr Opin Struct Biol. .

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.

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