| pubmed-article:19319935 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19319935 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:19319935 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:19319935 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:19319935 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:19319935 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:19319935 | lifeskim:mentions | umls-concept:C1433062 | lld:lifeskim |
| pubmed-article:19319935 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:19319935 | lifeskim:mentions | umls-concept:C0596448 | lld:lifeskim |
| pubmed-article:19319935 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:19319935 | pubmed:dateCreated | 2009-4-2 | lld:pubmed |
| pubmed-article:19319935 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19319935 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19319935 | 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. | lld:pubmed |
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| pubmed-article:19319935 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19319935 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19319935 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19319935 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19319935 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19319935 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19319935 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:19319935 | pubmed:issn | 1469-896X | lld:pubmed |
| pubmed-article:19319935 | pubmed:author | pubmed-author:OtteH PHP | lld:pubmed |
| pubmed-article:19319935 | pubmed:author | pubmed-author:TyoJ SJS | lld:pubmed |
| pubmed-article:19319935 | pubmed:author | pubmed-author:RaoZiheZ | lld:pubmed |
| pubmed-article:19319935 | pubmed:author | pubmed-author:ZhongNanN | lld:pubmed |
| pubmed-article:19319935 | pubmed:author | pubmed-author:LiangChaoC | lld:pubmed |
| pubmed-article:19319935 | pubmed:author | pubmed-author:XueFeiF | lld:pubmed |
| pubmed-article:19319935 | pubmed:author | pubmed-author:JinChangwenC | lld:pubmed |
| pubmed-article:19319935 | pubmed:author | pubmed-author:LouZhiyongZ | lld:pubmed |
| pubmed-article:19319935 | pubmed:author | pubmed-author:XueKangK | lld:pubmed |
| pubmed-article:19319935 | pubmed:author | pubmed-author:ZhangShengnan... | lld:pubmed |
| pubmed-article:19319935 | pubmed:author | pubmed-author:ChenJiaxuanJ | lld:pubmed |
| pubmed-article:19319935 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19319935 | pubmed:volume | 18 | lld:pubmed |
| pubmed-article:19319935 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19319935 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19319935 | pubmed:pagination | 839-44 | lld:pubmed |
| pubmed-article:19319935 | pubmed:dateRevised | 2010-9-23 | lld:pubmed |
| pubmed-article:19319935 | pubmed:meshHeading | pubmed-meshheading:19319935... | lld:pubmed |
| pubmed-article:19319935 | pubmed:meshHeading | pubmed-meshheading:19319935... | lld:pubmed |
| pubmed-article:19319935 | pubmed:meshHeading | pubmed-meshheading:19319935... | lld:pubmed |
| pubmed-article:19319935 | pubmed:meshHeading | pubmed-meshheading:19319935... | lld:pubmed |
| pubmed-article:19319935 | pubmed:meshHeading | pubmed-meshheading:19319935... | lld:pubmed |
| pubmed-article:19319935 | pubmed:meshHeading | pubmed-meshheading:19319935... | lld:pubmed |
| pubmed-article:19319935 | pubmed:meshHeading | pubmed-meshheading:19319935... | lld:pubmed |
| pubmed-article:19319935 | pubmed:meshHeading | pubmed-meshheading:19319935... | lld:pubmed |
| pubmed-article:19319935 | pubmed:meshHeading | pubmed-meshheading:19319935... | lld:pubmed |
| pubmed-article:19319935 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19319935 | pubmed:articleTitle | C-terminal domain of SARS-CoV main protease can form a 3D domain-swapped dimer. | lld:pubmed |
| pubmed-article:19319935 | pubmed:affiliation | Beijing Nuclear Magnetic Resonance Center, Peking University, Beijing 100871, People' Republic of China. | lld:pubmed |
| pubmed-article:19319935 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19319935 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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