Networks for the allosteric control of protein kinases
Current Opinion in Structural BiologyPublished 8 November 2006
Zhengshuang Shi, Katheryn A. Resing, Natalie G. Ahn
Citations78
SJR quartileQ1
SJR score2.91
SNIP1.48
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TL;DR
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.
Abstract
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.
Keywords
Materials ScienceBiochemistry, Genetics and Molecular Biology
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