pH-dependent conformational flexibility of the SARS-CoV main proteinase (Mpro) dimer: Molecular dynamics simulations and multiple X-ray structure analyses

Journal of Molecular Biology

Volumn 354, Issue 1, 2005, Pages 25-40

  Tan, Jinzhi ^a,b   Verschueren, Koen H G ^b   Anand, Kanchan ^b   Shen, Jianhua ^a   Yang, Maojun ^b   Xu, Yechun ^a   Rao, Zihe ^c,d   Bigalke, Janna ^b   Heisen, Burkhard ^b   Mesters, Jeroen R ^b   Chen, Kaixian ^a   Shen, Xu ^a   Jiang, Hualiang ^a   Hilgenfeld, Rolf ^b  

^a SHANGHAI INSTITUTE OF MATERIA MEDICA   (China)

^b UNIVERSITY OF LÜBECK   (Germany)

^c TSINGHUA UNIVERSITY   (China)

^d INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

Author keywords

Conformational flexibility; Molecular dynamics simulation; Multiple X ray structures; New crystal forms; SARS CoV Mpro

Indexed keywords

DIMER; HISTIDINE; MONOMER; PROTEINASE; VIRUS ENZYME;

ARTICLE; BINDING SITE; CALCULATION; CRYSTAL STRUCTURE; DIMERIZATION; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME SUBSTRATE; MOLECULAR DYNAMICS; NONHUMAN; PH; PRIORITY JOURNAL; PROTON TRANSPORT; SARS CORONAVIRUS; SIMULATION; STRUCTURE ANALYSIS; X RAY ANALYSIS;

SARS CORONAVIRUS; SARS COV;

EID: 27344443434     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.09.012     Document Type: Article

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