Lining the pockets of kinases and phosphatases.
作者： Matthew G Gold , David Barford , David Komander
DOI: 10.1016/J.SBI.2006.10.006
关键词:
摘要: The regulation of the activity kinases and phosphatases is an essential aspect intracellular signal transduction. Recently determined structures AGC protein kinases, including isoforms PKB, PKC, GRK ROCK, indicate that occupancy a hydrophobic pocket in kinase N-lobe by segment immediately C terminal to domain provides mechanism for regulating activity. In addition, crystal Aurora-A Aurora-B, which are closely related family complex with their activators, TPX2 INCENP, respectively, show how allosteric activation achieved binding activator equivalent pocket. Hence, analogous interactions shared regulatory these kinases. Two have explained molecular basis PKA anchoring through its subunits members AKAP scaffold proteins. AKAPs can also interact directly phosphatase catalytic domains. structure PP1 subunit targeting MYPT1 indicates there scope intimate
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