Networks for the allosteric control of protein kinases.
The allosteric regulation of protein kinases serves as an efficient strategy for molecular communication, event coupling and interconversion between catalytic states. Recent co-crystal structures have revealed novel ways in which kinases control activity and substrate specificity following phosphorylation, dimerization, or binding to regulatory proteins, substrates and scaffolds. In addition, hydrogen exchange coupled with mass spectrometry is emerging as a complementary strategy to probe the solution behavior of kinases; recent results have shown that allosteric regulation may involve transitions in protein motions as well as structural rearrangements.
Shi
Zhengshuang
Z
Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA.
Resing
Katheryn A
KA
Ahn
Natalie G
NG
D000494:Allosteric Regulation; D000495:Allosteric Site; D003903:Deuterium; D019281:Dimerization; D048049:Extracellular Signal-Regulated MAP Kinases / Q000737:chemistry / Q000378:metabolism; D006859:Hydrogen; D013058:Mass Spectrometry; D008954:Models, Biological; D008958:Models, Molecular; D011494:Protein Kinases / Q000737:chemistry* / Q000378:metabolism*; D020836:Protein Structure, Quaternary; D015398:Signal Transduction
D006859:Hydrogen; D003903:Deuterium; D011494:Protein Kinases; D048049:Extracellular Signal-Regulated MAP Kinases