Docking interactions in protein kinase and phosphatase networks.
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.
Reményi
Attila
A
Department of Cellular and Molecular Pharmacology, Program in Biological Sciences, University of California San Francisco, 600 16th Street, San Francisco, CA 94143-2240, USA.
Good
Matthew C
MC
Lim
Wendell A
WA
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
D046912:Multiprotein Complexes; D011494:Protein Kinases; D010749:Phosphoprotein Phosphatases