Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 16, Issue 6, Pages 686-692Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2006.10.011
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The allosteric regulation of protein kinases serves as an efficient strategy for molecular communication, event coupling and interconversion between catalytic states. Recent cocrystal structures have revealed novel ways in which kinases control activity and substrate specificity following phosphorylation, climerization, 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.
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