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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2009-4-2
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pubmed:databankReference |
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pubmed:abstractText |
SARS coronavirus main protease (M(pro)) plays an essential role in the extensive proteolytic processing of the viral polyproteins (pp1a and pp1ab), and it is an important target for anti-SARS drug development. We have reported that both the M(pro) C-terminal domain alone (M(pro)-C) and the N-finger deletion mutant of M(pro) (M(pro)-Delta7) exist as a stable dimer and a stable monomer (Zhong et al., J Virol 2008; 82:4227-4234). Here, we report structures of both M(pro)-C monomer and dimer. The structure of the M(pro)-C monomer is almost identical to that of the C-terminal domain in the crystal structure of M(pro). Interestingly, the M(pro)-C dimer structure is characterized by 3D domain-swapping, in which the first helices of the two protomers are interchanged and each is enwrapped by four other helices from the other protomer. Each folding subunit of the M(pro)-C domain-swapped dimer still has the same general fold as that of the M(pro)-C monomer. This special dimerization elucidates the structural basis for the observation that there is no exchange between monomeric and dimeric forms of M(pro)-C and M(pro)-Delta7.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19319935-10212987,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19319935-11224563,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19319935-12051947,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19319935-12093723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19319935-12746549,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19319935-12892955,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19319935-12917313,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19319935-12927536,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19319935-12928031,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19319935-14561748,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19319935-14585926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19319935-15037623,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19319935-15299926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19319935-15572765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19319935-16128623,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19319935-16200636,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19319935-17144656,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19319935-1737021,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19319935-18305043,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19319935-8019132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19319935-9367762
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1469-896X
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pubmed:author |
pubmed-author:ChenJiaxuanJ,
pubmed-author:JinChangwenC,
pubmed-author:LiangChaoC,
pubmed-author:LouZhiyongZ,
pubmed-author:OtteH PHP,
pubmed-author:RaoZiheZ,
pubmed-author:TyoJ SJS,
pubmed-author:XueFeiF,
pubmed-author:XueKangK,
pubmed-author:ZhangShengnanS,
pubmed-author:ZhongNanN
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pubmed:issnType |
Electronic
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
839-44
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pubmed:dateRevised |
2010-9-23
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pubmed:meshHeading |
pubmed-meshheading:19319935-Crystallography, X-Ray,
pubmed-meshheading:19319935-Cysteine Endopeptidases,
pubmed-meshheading:19319935-Humans,
pubmed-meshheading:19319935-Protein Conformation,
pubmed-meshheading:19319935-Protein Multimerization,
pubmed-meshheading:19319935-Protein Structure, Tertiary,
pubmed-meshheading:19319935-SARS Virus,
pubmed-meshheading:19319935-Viral Core Proteins,
pubmed-meshheading:19319935-Viral Proteins
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pubmed:year |
2009
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pubmed:articleTitle |
C-terminal domain of SARS-CoV main protease can form a 3D domain-swapped dimer.
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pubmed:affiliation |
Beijing Nuclear Magnetic Resonance Center, Peking University, Beijing 100871, People' Republic of China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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