A Comparative CEST NMR Study of Slow Conformational Dynamics of Small GTPases Complexed with GTP and GTP Analogues

被引：38

作者：

Long, Dong ^{[1
,2
,3
]}

Marshall, Christopher B. ^{[4
]}

Bouvignies, Guillaume ^{[1
,2
,3
]}

Mazhab-Jafari, Mohammad T. ^{[4
]}

Smith, Matthew J. ^{[4
]}

Ikura, Mitsuhiko ^{[4
]}

Kay, Lewis E. ^{[1
,2
,3
]}

机构：

[1] Univ Toronto, Dept Mol Genet, Toronto, ON M5S 1A8, Canada

[2] Univ Toronto, Dept Biochem, Toronto, ON M5S 1A8, Canada

[3] Univ Toronto, Dept Chem, Toronto, ON M5S 1A8, Canada

[4] Univ Toronto, Deparment Med Biophys, Univ Hlth Network, Ontario Canc Inst, Toronto, ON M5S 1A8, Canada

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2013年 / 52卷 / 41期

基金：

加拿大健康研究院; 加拿大自然科学与工程研究理事会;

关键词：

conformational dynamics; enzymes; NMR spectroscopy; protein dynamics; proteins; RAS PROTEIN; EFFECTOR INTERACTION; STRUCTURAL BASIS; BINDING; STATES; EXCHANGE; MODULATION;

D O I：

10.1002/anie.201305434

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Conformational Exchange: Small GTPases, such as Ras and Rheb, exchange between major and minor conformers when bound to GTP, with different functional properties for each state (see picture). Two-dimensional 15N CEST NMR spectroscopy is used to quantify the exchange parameters for both Ras and Rheb complexed with physiological GTP and the analogues GTPγS and GppNHp. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：10771 / 10774

页数：4

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