淡江大學機構典藏:Item 987654321/91703
English  |  正體中文  |  简体中文  |  全文笔数/总笔数 : 62830/95882 (66%)
造访人次 : 4036599      在线人数 : 635
RC Version 7.0 © Powered By DSPACE, MIT. Enhanced by NTU Library & TKU Library IR team.
搜寻范围 查询小技巧：
  • 您可在西文检索词汇前后加上"双引号"，以获取较精准的检索结果
  • 若欲以作者姓名搜寻，建议至进阶搜寻限定作者字段，可获得较完整数据
    •  进阶搜寻


    jsp.display-item.identifier=請使用永久網址來引用或連結此文件: https://tkuir.lib.tku.edu.tw/dspace/handle/987654321/91703


    题名: Mechanism for controlling the monomer–dimer conversion of SARS coronavirus main protease
    作者: Wu, Cheng-Guo;Cheng, Shu-Chun;Chen, Shiang-Chuan;Li, Juo-Yan;Fang, Yi-Hsuan;Chen, Yau-Hung;Chou, Chi-Yuan
    贡献者: 淡江大學生命科學研究所
    关键词: SARS;SARS coronavirus;main protease
    日期: 2013-05-01
    上传时间: 2013-07-29 09:24:21 (UTC+8)
    出版者: Malden: Wiley-Blackwell Publishing, Inc.
    摘要: The Severe acute respiratory syndrome coronavirus (SARS-CoV) main protease (Mpro) cleaves two virion polyproteins (pp1a and pp1ab); this essential process represents an attractive target for the development of anti-SARS drugs. The functional unit of Mpro is a homodimer and each subunit contains a His41/Cys145 catalytic dyad. Large amounts of biochemical and structural information are available on Mpro; nevertheless, the mechanism by which monomeric Mpro is converted into a dimer during maturation still remains poorly understood. Previous studies have suggested that a C-terminal residue, Arg298, interacts with Ser123 of the other monomer in the dimer, and mutation of Arg298 results in a monomeric structure with a collapsed substrate-binding pocket. Interestingly, the R298A mutant of Mpro shows a reversible substrate-induced dimerization that is essential for catalysis. Here, the conformational change that occurs during substrate-induced dimerization is delineated by X-ray crystallography. A dimer with a mutual orientation of the monomers that differs from that of the wild-type protease is present in the asymmetric unit. The presence of a complete substrate-binding pocket and oxyanion hole in both protomers suggests that they are both catalytically active, while the two domain IIIs show minor reorganization. This structural information offers valuable insights into the molecular mechanism associated with substrate-induced dimerization and has important implications with respect to the maturation of the enzyme.
    關聯: Acta Crystallographica Section D Biological Crystallography 69(5), pp.747-755
    DOI: 10.1107/S0907444913001315
    显示于类别:[化學學系暨研究所] 期刊論文

    文件中的档案:

    档案 描述 大小格式浏览次数
    2013 ACTA D-P.pdf1884KbAdobe PDF634检视/开启
    index.html0KbHTML303检视/开启

    在機構典藏中所有的数据项都受到原著作权保护.

    TAIR相关文章

    DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library & TKU Library IR teams. Copyright ©   - 回馈