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The structural basis for substrate recognition and control by protein kinases 1
Author(s) -
Johnson Louise N,
Lowe Edward D,
Noble Martin E.M,
Owen David J
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00606-1
Subject(s) - cyclin dependent kinase 2 , mitogen activated protein kinase kinase , cyclin dependent kinase 9 , receptor tyrosine kinase , biochemistry , map2k7 , g protein coupled receptor kinase , proto oncogene tyrosine protein kinase src , chemistry , map kinase kinase kinase , ask1 , kinase , sh3 domain , tyrosine kinase , biology , microbiology and biotechnology , protein kinase a , signal transduction , g protein coupled receptor
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 of 12 protein kinases are now known. These include structures of kinases in the active state in ternary complexes with ATP (or analogues) and inhibitor or peptide substrates (e.g. cyclic AMP dependent protein kinase, phosphorylase kinase and insulin receptor tyrosine kinase); kinases in both active and inactive states (e.g. CDK2/cyclin A, insulin receptor tyrosine kinase and MAPK); kinases in the active state (e.g. casein kinase 1, Lck); and kinases in inactive states (e.g. twitchin kinase, calcium calmodulin kinase 1, FGF receptor kinase, c‐Src and Hck). This paper summarises the detailed information obtained with active phosphorylase kinase ternary complex and reviews the results with reference to other kinase structures for insights into mechanisms for substrate recognition and control.