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
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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
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