1. Molecular basis for p38 protein kinase inhibitor specificity
- Author
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Lisnock, JeanMarie, Tebben, Andy, Frantz, Betsy, O'Neill, Edward A., Croft, Gist, O'Keefe, Stephen J., Li, Bing, Hacker, Candice, Laszlo, Stephen de, Smith, Anthony, Libby, Brian, Liverton, Nigel, Hermes, Jeffrey, and LoGrasso, Philip
- Subjects
Cooperative binding (Biochemistry) -- Research ,Enzyme inhibitors -- Research ,Enzymes -- Structure-activity relationship ,Protein kinases -- Physiological aspects ,Biological sciences ,Chemistry - Abstract
A study relating to the investigation of serine/threonine kinases and tyrosine kinases was conducted to determine what residues in the critical enzyme and mitrogen-activated protein kinase p38 were essential for inhibitor binding using site-directed mutagenesis. Among the major results of the study, it was found that threonine 106 is a major determinant for p38 inhibitor specificity and methionin 109 contributes to increased binding affinity for the diarylimidazoles.
- Published
- 1998