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蛋白质柔性区间的预测方法研究进展 被引量:4

Advances in the Research on the Methods of Prediction of the Flexible Rigions in Protein
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摘要 蛋白质的柔性区间是蛋白质与其它分子结合所必需的结构,是蛋白质发挥正常功能的关键因素。不同的预测方法对柔性区间的定义有所不同。文章试图对几种较为重要的预测方法进行简要的介绍。 The flexible rigion plays the key role in the motion of molecular and the normal function of protein. For example, the activity of most enzymes depends on the flexible rigion, and the conformation of the flexible rigion usually determines the 3D-structure of the entire molecule. Besides, the application of the flexible rigion also means a lot in the Computer-Assisted Drug-Design. Thus the prediction of the flexible rigion of protein becomes one of the most interesting areas in the research of bioinformatics. The methods of prediction of the flexible tiglon of protein still need to be studied, which include the experimental method and bioinformatic method. The bioinformatic method is cheaper and more conveniet than the other methods, so it becomes the most hopeful in the future. The prediction of flexible tiglon of protein by the bioinformatic method started in 1980s. Many algorithms have been used in the prediction. But different algorithms do not get the same result because of different definition of the flexible rigion in potein. Predicting with the help of URMSD is very popular nowadays. This article tries to explain several definitions of flexible rigions in protein, and to introduce the development of bioinformatic method in the prediction and a few important algorithms in the prediction.
出处 《药物生物技术》 CAS CSCD 2009年第6期578-581,共4页 Pharmaceutical Biotechnology
关键词 蛋白质柔性区间 预测方法 均方根距离的单位向量 Flexible rigions in protein, Methods of prediction, URMSD
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  • 1Yap KL, Yuan T, Mal TK, etal. Structural basis for simultaneous binding of two carboxy terminal peptides of plant glutamate decarhoxylase to calmodulin [J]. J Mol Biog, 2003,328:193.
  • 2Schurnacher MA, Rivard AF, Bachinger HP, et al. Structure of the gating domain of a Ca^2+-activated K^+ channel cornplexed with Ca^2+/calrnodulin[J ]. Nature, 2001, 410 : 1120.
  • 3Chen K, Ruan J, Kurgan LA. Prediction of three dimensional structure of cahnodulin[J]. Protein J, 2006,25: 57.
  • 4Carney DS, Davies BA, Horazdovsky BF. Vps9 domain-containing proteins: activators of Rab5 GTPases from yeast to neurons[J]. Trends Cell Biol, 2006,16 : 27.
  • 5Yeagle PL, Albert AD. A conformational trigger for activation of a G protein by a G protein-coupled receptor[J]. Biochemistry, 2003,42:1365.
  • 6King AE, Ackley MA, Cass CE, et al. Nueleoside transporters: from scavengers to novel therapeutic targets[J]. Trends Pharmacol Sci , 2006,27:416.
  • 7Fitzgerald KA, Chen ZJ. Sorting out Toll signals[J]. Cell, 2006,125 : 834.
  • 8Ruan J, Chen K, Tuszynski J, et al. Quantitative Analysis of the Conservation of the Tertiary Structure of Protein Segments[J]. Protein J, 2006,25(5) :301.
  • 9Kofler MM, Freund C. The GYF domain[J]. FEBS J, 2006,273: 245.
  • 10Zaman MH, Kaazempur-Mofrad MR. How flexible is alphaactinin's rod domain? [J]. Mech Chern Biosyst, 2004,1 : 291.

二级参考文献22

  • 1Nathan AB, David S, Simpson J, et al. Electrostatics of nanosystems: application to microtubules and the ribosome[J]. Proc Natl Acad Sci USA, 2001, 98(18) : 10037.
  • 2Hans JB. Ludi-rule-based automatic design of substituents for enzyme-inhibitor leads [J]. CompwAided Mol Des, 1992, 6(6):593.
  • 3Hans JB. The Computer-Program Ludi a new method for the denovo design of enzyme-inhibitors[J]. CompwAided Mol Des, 1992, 6(1):593.
  • 4Robert SD, Eugene IS. SMOG: de novo design method based on simple, fast, and accurate free energy estimates. 1. Methodology and supporting evidence [J]. Am Chem Soc, 1996, 118(47) :11733.
  • 5O'hearn SD, Kusalik AJ, Angel Jf. MolCom: a method to compare protein molecules based on 3-D structural and chemical similarity[J]. Protein Eng, 2003, 16(3) : 169.
  • 6Vadim A, Ursula L, Nathaniel E, et al. Normal modes for predicting protein motions: a comprehensive database assessment and associated Web tool[J]. Protein Sci, 2005, 14:633.
  • 7Buyong M, Tal E, Haim W, et al. Protein-Protein interactions: structurally conserved residues distinguish between binding sites and exposed protein surfaces[J]. Proc Natl Acad Sci USA, 2003, 100(10) : 5772.
  • 8Xiang L, Ozlem K, Buyong M, et al. Protein-protein interactions: hot spots and structurally conserved residues often located in complemented pockets that pre-organized in the unbound states: implications for docking [J]. J Mol Biol, 2004, 344(3) :781.
  • 9Cyril D, Alexandre MJJB, Frederik MAS, et al. Structural model of the UbcHSB/CNOT4 complex revealed by combining NMR, mutagenesis and docking approaches[J] Structure, 2004, 12(4):633.
  • 10Graham RS, Paul WF, Christopher SP, etal. Incorporation of flexdbility into rigid-body docking: applications in rounds 3-5 of CAPRI[J].Proteins, 2005, 60(2):263.

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