Regulation of protein kinases; controlling activity through activation segment conformation.
There are currently at least forty-six unique protein kinase crystal structures, twenty-four of which are available in an active state. Here we examine these structures using a structural bioinformatics approach to understand how the conformation of the activation segment controls kinase activity.
Nolen
Brad
B
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92116, USA.
Taylor
Susan
S
Ghosh
Gourisankar
G
D020816:Amino Acid Motifs / Q000502:physiology; D000818:Animals; D020134:Catalytic Domain / Q000502:physiology; D019295:Computational Biology; D006801:Humans; D008958:Models, Molecular; D008968:Molecular Conformation; D010766:Phosphorylation; D011494:Protein Kinases / Q000737:chemistry*; D017434:Protein Structure, Tertiary / Q000502:physiology; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
D011494:Protein Kinases