title: Docking interactions in protein kinase and phosphatase networks.
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.
authors.affiliation: Department of Cellular and Molecular Pharmacology, Program in Biological Sciences, University of California San Francisco, 600 16th Street, San Francisco, CA 94143-2240, USA.
authors.forename: Attila
authors.initials: A
authors.lastname: Reményi
authors.forename: Matthew C
authors.initials: MC
authors.lastname: Good
authors.forename: Wendell A
authors.initials: WA
authors.lastname: Lim
mesh_terms: D000494:Allosteric Regulation; D001665:Binding Sites; D015195:Drug Design; D020935:MAP Kinase Signaling System; D008954:Models, Biological; D008958:Models, Molecular; D046912:Multiprotein Complexes; D010749:Phosphoprotein Phosphatases / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D011494:Protein Kinases / Q000737:chemistry* / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D015398:Signal Transduction
chemical_list: D046912:Multiprotein Complexes; D011494:Protein Kinases; D010749:Phosphoprotein Phosphatases