title: Regulation of protein kinases; controlling activity through activation segment conformation.
abstract: 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.
authors.affiliation: Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92116, USA.
authors.forename: Brad
authors.initials: B
authors.lastname: Nolen
authors.forename: Susan
authors.initials: S
authors.lastname: Taylor
authors.forename: Gourisankar
authors.initials: G
authors.lastname: Ghosh
mesh_terms: 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
chemical_list: D011494:Protein Kinases