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DRSP:蛋白质单残基替换结构数据库
引用本文:刘继龙,苗智超,李雷,肖智雄,曹洋.DRSP:蛋白质单残基替换结构数据库[J].生物化学与生物物理进展,2016,43(8):810-816.
作者姓名:刘继龙  苗智超  李雷  肖智雄  曹洋
作者单位:四川大学生命科学学院,生物资源与生态环境教育部重点实验室,生长代谢衰老研究中心, 成都, 610064,Architecture and Reactivity of the RNA, University of Strasbourg, Institute of Molecular and Celluar Biology of CNRS 67000 Strasbourg France,四川大学生命科学学院,生物资源与生态环境教育部重点实验室,生长代谢衰老研究中心, 成都, 610064,四川大学生命科学学院,生物资源与生态环境教育部重点实验室,生长代谢衰老研究中心, 成都, 610064,四川大学生命科学学院,生物资源与生态环境教育部重点实验室,生长代谢衰老研究中心, 成都, 610064
基金项目:国家自然科学基金(31401130)和生物大分子国家重点实验室开放研究课题(2014kf 04)
摘    要:蛋白质残基替换是基因突变的产物之一,它可能改变蛋白质三维结构,对其生物学功能产生重大影响,因此研究蛋白质残基替换与结构改变的关系具有重要意义.随着实验解析蛋白质结构的数量迅猛增长,越来越多的野生型-突变体被应用于结构生物学的比较研究中.本研究从蛋白质三维结构数据库(PDB)出发,收集和计算了大量结构特征数据,构建了一个目前已知最大的野生型-突变体(单残基差异)的结构对数据库DRSP,展示出氨基酸类型和主链偏好性对结构保守性的相关性.DRSP的开放使用可为高精度的蛋白质结构分析预测提供有用信息,它的数据库网址是http://www.labshare.cn/drsp/index.php.

关 键 词:数据库,蛋白质残基替换,主链柔性,蛋白质结构预测,蛋白质设计
收稿时间:2016/2/23 0:00:00
修稿时间:2016/5/27 0:00:00

DRSP: a Structural Database for Single Residue Substitutions in PDB
LIU Ji-Long,MIAO Zhi-Chao,LI Lei,XIAO Zhi-Xiong and CAO Yang.DRSP: a Structural Database for Single Residue Substitutions in PDB[J].Progress In Biochemistry and Biophysics,2016,43(8):810-816.
Authors:LIU Ji-Long  MIAO Zhi-Chao  LI Lei  XIAO Zhi-Xiong and CAO Yang
Institution:Center for Growth, Metabolism and Aging, Key Laboratory of Biological Resources and Ecological Environment of Ministry of Education, College of Life Sciences, Sichuan University, Chengdu 610064, China,Architecture and Reactivity of the RNA, University of Strasbourg, Institute of Molecular and Celluar Biology of CNRS 67000 Strasbourg France,Center for Growth, Metabolism and Aging, Key Laboratory of Biological Resources and Ecological Environment of Ministry of Education, College of Life Sciences, Sichuan University, Chengdu 610064, China,Center for Growth, Metabolism and Aging, Key Laboratory of Biological Resources and Ecological Environment of Ministry of Education, College of Life Sciences, Sichuan University, Chengdu 610064, China and Center for Growth, Metabolism and Aging, Key Laboratory of Biological Resources and Ecological Environment of Ministry of Education, College of Life Sciences, Sichuan University, Chengdu 610064, China
Abstract:Substitutions of residues introduced by gene mutations can impact protein structures and often alternate protein properties. Identifying substitution-related structural changes is crucial for understanding their effects in biological functions. With the explosive numbers of experimentally determined protein structures, more and more wild-type-mutant structures have been used in comparable studies of structural biology. In this work, we constructed a structure-pair database, named DRSP, which collected non-redundant pairs of proteins with single residue substitutions in the entire Protein Data Bank. DRSP demonstrates abundant information for mutant-structure prediction and protein design. More importantly, DRSP presents the superimposed pairs of wild-type-mutant structures for backbone-perturbation studies, which are very important for the highly accurate structure modeling. DRSP is available at http:// www.labshare.cn/drsp/index.php.
Keywords:database  protein residue substitution  backbone flexibility  protein structure prediction  protein design
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