The conformational plasticity of protein kinases.
Protein kinases operate in a large number of distinct signaling pathways, where the tight regulation of their catalytic activity is crucial to the development and maintenance of eukaryotic organisms. The catalytic domains of different kinases adopt strikingly similar structures when they are active. By contrast, crystal structures of inactive kinases have revealed a remarkable plasticity in the kinase domain that allows the adoption of distinct conformations in response to interactions with specific regulatory domains or proteins.
Huse
Morgan
M
Department of Biological Sciences, Stanford University, Palo Alto, California 94305, USA.
Kuriyan
John
J
D000818:Animals; D020134:Catalytic Domain / Q000502:physiology; D004789:Enzyme Activation; D005057:Eukaryotic Cells / Q000201:enzymology; D008958:Models, Molecular; D011487:Protein Conformation; D011494:Protein Kinases / Q000737:chemistry / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D020794:Receptor Protein-Tyrosine Kinases / Q000378:metabolism; D036183:Receptor, EphB2; D000077293:Receptor, Transforming Growth Factor-beta Type I; D018125:Receptors, Transforming Growth Factor beta; D015398:Signal Transduction; D013379:Substrate Specificity
D018125:Receptors, Transforming Growth Factor beta; D011494:Protein Kinases; D020794:Receptor Protein-Tyrosine Kinases; D036183:Receptor, EphB2; D017346:Protein Serine-Threonine Kinases; D000077293:Receptor, Transforming Growth Factor-beta Type I