期刊
FEBS LETTERS
卷 578, 期 3, 页码 305-310出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2004.11.020
关键词
Ras; conformational dynamics; effector interaction; P-31 NMR spectroscopy
Ras regulates a variety of different signal transduction pathways acting as molecular switch. It was shown by liquid and solid-state P-31 NMR spectroscopy that Ras exists in the guanosine-5'-(beta, gamma-imido)triphosphate bound form in at least two conformational states interconverting in millisecond time scale. The relative population between the two conformational states affects drastically the affinity of Ras to its effectors. P-31 NMR spectroscopy shows that the conformational equilibrium can be shifted specifically by point mutations, including mutations with oncogenic potential, thus modifying the effector interactions and their coupling to dynamic properties of the protein. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据