Journal
BIOLOGICAL CHEMISTRY
Volume 393, Issue 10, Pages 1121-1129Publisher
WALTER DE GRUYTER & CO
DOI: 10.1515/hsz-2012-0248
Keywords
anticancer; crystallography; drug design; phosphotransferase; surrogate
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Funding
- Norwegian Cancer Society
- Norwegian Research Council
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The era of structure-based protein kinase inhibitor design began in the early 1990s with the determination of crystal structures of protein kinase A (PKA, or cyclic AMP-dependent kinase). Although many other protein kinases have since been extensively characterized, PKA remains a prototype for studies of protein kinase active conformations. It serves well as a model for the structural properties of AGC subfamily protein kinases, clarifying inhibitor selectivity profiles. Its reliable expression, constitutive activity, simple domain structure, and reproducible crystallizability have also made it a useful surrogate for the discovery of inhibitors of both established and emerging AGC kinase targets.
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