title: Domain movements in protein kinases.
abstract: Structural studies of the catalytic subunit of the cAMP-dependent protein kinase, both by crystallographic methods and in solution, reveal two conformations. Crystal structures of several other protein kinases have also been solved in the past year. With this combined information we can begin to define mobile domains and subdomains within the conserved catalytic core.
authors.affiliation: Department of Chemistry and Biochemistry, University of California at San Diego, La Jolla 92093-0654.
authors.forename: S
authors.initials: S
authors.lastname: Cox
authors.forename: E
authors.initials: E
authors.lastname: Radzio-Andzelm
authors.forename: S S
authors.initials: SS
authors.lastname: Taylor
mesh_terms: D000818:Animals; D001665:Binding Sites; D002352:Carrier Proteins / Q000378:metabolism; D047908:Intracellular Signaling Peptides and Proteins; D008958:Models, Molecular; D011487:Protein Conformation; D047428:Protein Kinase Inhibitors; D011494:Protein Kinases / Q000737:chemistry* / Q000378:metabolism
chemical_list: D002352:Carrier Proteins; D047908:Intracellular Signaling Peptides and Proteins; D047428:Protein Kinase Inhibitors; C015482:protein kinase modulator; D011494:Protein Kinases