Department of Biochemistry, The University of Colorado at Boulder, USA.
Department of Biochemistry, The University of Colorado at Boulder, USA.
Curr Opin Struct Biol. 2021 Dec;71:215-222. doi: 10.1016/j.sbi.2021.07.006. Epub 2021 Aug 20.
Structural changes involved in protein kinase activation and ligand binding have been determined from a wealth of X-ray crystallographic evidence. Recent solution studies using NMR, EPR, HX-MS, and fluorescence techniques have deepened this understanding by highlighting the underlying energetics and dynamics of multistate conformational ensembles. This new research is showing how activation mechanisms and ligand binding alter the internal motions of kinases and enable allosteric coupling between distal regulatory regions and the active site.
从大量的 X 射线晶体学证据中确定了蛋白激酶激活和配体结合涉及的结构变化。最近使用 NMR、EPR、HX-MS 和荧光技术的溶液研究通过突出多态构象集合的潜在能量和动力学，加深了对此的理解。这项新的研究表明激活机制和配体结合如何改变激酶的内部运动，并使远端调节区域和活性位点之间的变构偶联成为可能。
