The structural basis for substrate recognition and control by protein kinases 1
作者： Louise N Johnson , Edward D Lowe , Martin E.M Noble , David J Owen
DOI: 10.1016/S0014-5793(98)00606-1
关键词:
摘要: Protein kinases catalyse phospho transfer reactions from ATP to serine, threonine or tyrosine residues in target substrates and provide key mechanisms for control of cellular signalling processes. The crystal structures 12 protein are now known. These include the active state ternary complexes with (or analogues) inhibitor peptide (e.g. cyclic AMP dependent kinase, phosphorylase kinase insulin receptor kinase); both inactive states CDK2/cyclin A, MAPK); casein 1, Lck); twitchin calcium calmodulin FGF c-Src Hck). This paper summarises detailed information obtained complex reviews results reference other insights into substrate recognition control.
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