Shi Zhengshuang, Resing Katheryn A, Ahn Natalie G
Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA.
Curr Opin Struct Biol. 2006 Dec;16(6):686-92. doi: 10.1016/j.sbi.2006.10.011. Epub 2006 Nov 7.
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.
蛋白激酶的变构调节是分子通讯、事件偶联以及催化状态间相互转换的有效策略。近期的共晶体结构揭示了激酶在磷酸化、二聚化或与调节蛋白、底物及支架结合后控制活性和底物特异性的新方式。此外，氢交换与质谱联用正成为探究激酶溶液行为的一种补充策略；最近的结果表明，变构调节可能涉及蛋白质运动的转变以及结构重排。
