Large conformational changes in proteins: signaling and other functions

被引：171

作者：

Grant, Barry J. ^{[1
,2
]}

Gorfe, Alemayehu A. ^{[5
]}

McCammon, J. Andrew ^{[1
,2
,3
,4
]}

机构：

[1] Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA

[2] Univ Calif San Diego, Ctr Theoret Biol Phys, La Jolla, CA 92093 USA

[3] Univ Calif San Diego, Howard Hughes Med Inst, La Jolla, CA 92093 USA

[4] Univ Calif San Diego, Dept Pharmacol, La Jolla, CA 92093 USA

[5] Univ Texas Hlth Sci Ctr Houston, Dept Integrat Biol & Pharmacol, Houston, TX USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2010年 / 20卷 / 02期

基金：

美国国家科学基金会; 美国国家卫生研究院;

关键词：

NORMAL-MODE ANALYSIS; MOLECULAR-DYNAMICS SIMULATION; SRC KINASE HCK; ATOMISTIC SIMULATIONS; BIOMOLECULAR SYSTEMS; CATALYTIC DOMAIN; TYROSINE KINASE; RAS; ACTIVATION; BINDING;

D O I：

10.1016/j.sbi.2009.12.004

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Guanine and adenine nucleotide triphosphatases, such as Ras proteins and protein kinases, undergo large conformational changes upon ligand binding in the course of their functions. New computer simulation methods have combined with experimental studies to deepen our understanding of these phenomena. In particular, a 'conformational selection' picture is emerging, where alterations in the relative populations of preexisting conformations can best describe the conformational switching activity of these important proteins.

引用

页码：142 / 147

页数：6

共 59 条

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