中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Molecular dynamics simulation of SRP GTPases: Towards an understanding of the complex formation from equilibrium fluctuations

文献类型:期刊论文

作者Yang, Mingjun1; Zhang, Xin2; Han, Keli1
刊名proteins-structure function and bioinformatics
出版日期2010-08-01
卷号78期号:10页码:2222-2237
关键词signal recognition particle correlation analysis principal component analysis overlap coefficient protein targeting reaction protein-protein interaction
产权排序1;1
通讯作者韩克利
英文摘要signal recognition particle (srp) and its receptor (sr) play essential role in the srp-dependent protein targeting pathway. they interact with one another to precisely regulate the targeting reaction. the mechanism of this interaction consists of at least two discrete conformational states: complex formation and gtpase activation. although structural studies have provided valuable insights into the understanding of the srp-sr interaction, it still remains unclear that how srp and sr gtpases use their intrinsic conformational flexibilities to exert multiple allosteric regulations on this interaction process. here, we use computational simulations to present the dynamic behavior of the srp gtpases at an atomic level to gain further understanding of srp-sr interaction. we show that: (i) equilibrium conformational fluctuations contain a cooperative inter- and intradomain structural rearrangements that are functionally relevant to complex formation, (ii) a series of residues in different domains are identified to correlate with each other during conformational rearrangements, and (iii) alpha 3 and alpha 4 helices at domain interface actively rearrange their relative conformation to function as a bridge between the n domain and the core region of the g domain. these results, in addition to structural studies, would harness our understanding of the molecular mechanism for srp and sr interaction. proteins 2010; 78:2222-2237. (c) 2010 wiley-liss, inc.
WOS标题词science & technology ; life sciences & biomedicine
类目[WOS]biochemistry & molecular biology ; biophysics
研究领域[WOS]biochemistry & molecular biology ; biophysics
关键词[WOS]signal-recognition-particle ; escherichia-coli ; conformational-changes ; protein translocation ; endoplasmic-reticulum ; allosteric mechanism ; membrane association ; guanine-nucleotides ; crystal-structure ; receptor ftsy
收录类别SCI
原文出处false
语种英语
WOS记录号WOS:000279387400004
公开日期2010-11-30
源URL[http://159.226.238.44/handle/321008/103261]  
专题大连化学物理研究所_中国科学院大连化学物理研究所
作者单位1.Chinese Acad Sci, Dalian Inst Chem Phys, State Key Lab Mol React Dynam, Dalian 116023, Liaoning, Peoples R China
2.CALTECH, Div Chem & Chem Engn, Pasadena, CA 91125 USA
推荐引用方式
GB/T 7714
Yang, Mingjun,Zhang, Xin,Han, Keli. Molecular dynamics simulation of SRP GTPases: Towards an understanding of the complex formation from equilibrium fluctuations[J]. proteins-structure function and bioinformatics,2010,78(10):2222-2237.
APA Yang, Mingjun,Zhang, Xin,&Han, Keli.(2010).Molecular dynamics simulation of SRP GTPases: Towards an understanding of the complex formation from equilibrium fluctuations.proteins-structure function and bioinformatics,78(10),2222-2237.
MLA Yang, Mingjun,et al."Molecular dynamics simulation of SRP GTPases: Towards an understanding of the complex formation from equilibrium fluctuations".proteins-structure function and bioinformatics 78.10(2010):2222-2237.

入库方式: OAI收割

来源:大连化学物理研究所

浏览0
下载0
收藏0
其他版本

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。