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题名: Molecular dynamics simulation of SRP GTPases: Towards an understanding of the complex formation from equilibrium fluctuations
作者: Yang, Mingjun1;  Zhang, Xin2;  Han, Keli1
通讯作者: 韩克利
关键词: signal recognition particle ;  correlation analysis ;  principal component analysis ;  overlap coefficient ;  protein targeting reaction ;  protein-protein interaction
刊名: PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
发表日期: 2010-08-01
DOI: 10.1002/prot.22734
卷: 78, 期:10, 页:2222-2237
收录类别: SCI
文章类型: Article
部门归属: 11
项目归属: 1101
产权排名: 1;1
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
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.
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
语种: 英语
原文出处: 查看原文
WOS记录号: WOS:000279387400004
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/103261
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

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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

Recommended Citation:
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.
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