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Protein kinases — structure and function
Author(s) -
Bossemeyer Dirk
Publication year - 1995
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 - 10.1016/0014-5793(95)00580-3
Subject(s) - kinase , chemistry , function (biology) , microbiology and biotechnology , biochemistry , biology
The solution of crystal structures from half a dozen protein kinases during the last four years in different laboratories has deepened our understanding of the catalysis and regulation of this enzyme class, and given a vigorous impetus to the whole field. Due to the great degree of sequence conservation among protein kinases the informational yield with every new structure is high, as each is a representative of the enzyme family in general and most often of a subclass in particular. This review will focus on the active site structure of cAMP‐dependent protein kinase (cAPK) with special regard to two new crystal structures; one of an active protein kinase CK1∗, which may represent an as yet unsolved step in the kinetic pathway, and the other of the insulin receptor kinase domain, the first structure of a tyrosine kinase.