C-terminal domain of SARS-CoV main protease can form a 3D domain-swapped dimer.
Identifieur interne : 002B69 ( Main/Exploration ); précédent : 002B68; suivant : 002B70C-terminal domain of SARS-CoV main protease can form a 3D domain-swapped dimer.
Auteurs : Nan Zhong [République populaire de Chine] ; Shengnan Zhang ; Fei Xue ; Xue Kang ; Peng Zou ; Jiaxuan Chen ; Chao Liang ; Zihe Rao ; Changwen Jin ; Zhiyong Lou ; Bin XiaSource :
- Protein science : a publication of the Protein Society [ 1469-896X ] ; 2009.
Descripteurs français
- KwdFr :
- Conformation des protéines, Cristallographie aux rayons X, Cysteine endopeptidases (), Cysteine endopeptidases (métabolisme), Humains, Multimérisation de protéines, Protéines du core viral (), Protéines du core viral (métabolisme), Protéines virales (), Protéines virales (métabolisme), Structure tertiaire des protéines, Virus du SRAS (enzymologie).
- MESH :
- enzymologie : Virus du SRAS.
- métabolisme : Cysteine endopeptidases, Protéines du core viral, Protéines virales.
- Conformation des protéines, Cristallographie aux rayons X, Cysteine endopeptidases, Humains, Multimérisation de protéines, Protéines du core viral, Protéines virales, Structure tertiaire des protéines.
English descriptors
- KwdEn :
- Crystallography, X-Ray, Cysteine Endopeptidases (chemistry), Cysteine Endopeptidases (metabolism), Humans, Protein Conformation, Protein Multimerization, Protein Structure, Tertiary, SARS Virus (enzymology), Viral Core Proteins (chemistry), Viral Core Proteins (metabolism), Viral Proteins (chemistry), Viral Proteins (metabolism).
- MESH :
- chemical , chemistry : Cysteine Endopeptidases, Viral Core Proteins, Viral Proteins.
- chemical , metabolism : Cysteine Endopeptidases, Viral Core Proteins, Viral Proteins.
- enzymology : SARS Virus.
- Crystallography, X-Ray, Humans, Protein Conformation, Protein Multimerization, Protein Structure, Tertiary.
Abstract
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.
DOI: 10.1002/pro.76
PubMed: 19319935
Affiliations:
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Le document en format XML
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sortKey="Zhang, Shengnan" sort="Zhang, Shengnan" uniqKey="Zhang S" first="Shengnan" last="Zhang">Shengnan Zhang</name></author><author><name sortKey="Xue, Fei" sort="Xue, Fei" uniqKey="Xue F" first="Fei" last="Xue">Fei Xue</name></author><author><name sortKey="Kang, Xue" sort="Kang, Xue" uniqKey="Kang X" first="Xue" last="Kang">Xue Kang</name></author><author><name sortKey="Zou, Peng" sort="Zou, Peng" uniqKey="Zou P" first="Peng" last="Zou">Peng Zou</name></author><author><name sortKey="Chen, Jiaxuan" sort="Chen, Jiaxuan" uniqKey="Chen J" first="Jiaxuan" last="Chen">Jiaxuan Chen</name></author><author><name sortKey="Liang, Chao" sort="Liang, Chao" uniqKey="Liang C" first="Chao" last="Liang">Chao Liang</name></author><author><name sortKey="Rao, Zihe" sort="Rao, Zihe" uniqKey="Rao Z" first="Zihe" last="Rao">Zihe Rao</name></author><author><name sortKey="Jin, Changwen" sort="Jin, Changwen" uniqKey="Jin C" first="Changwen" last="Jin">Changwen Jin</name></author><author><name sortKey="Lou, Zhiyong" sort="Lou, Zhiyong" uniqKey="Lou Z" first="Zhiyong" last="Lou">Zhiyong Lou</name></author><author><name sortKey="Xia, Bin" sort="Xia, Bin" uniqKey="Xia B" first="Bin" last="Xia">Bin Xia</name></author></analytic><series><title level="j">Protein science : a publication of the Protein Society</title><idno type="eISSN">1469-896X</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Crystallography, X-Ray</term><term>Cysteine Endopeptidases (chemistry)</term><term>Cysteine Endopeptidases (metabolism)</term><term>Humans</term><term>Protein Conformation</term><term>Protein Multimerization</term><term>Protein Structure, Tertiary</term><term>SARS Virus (enzymology)</term><term>Viral Core Proteins (chemistry)</term><term>Viral Core Proteins (metabolism)</term><term>Viral Proteins (chemistry)</term><term>Viral Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Cysteine endopeptidases ()</term><term>Cysteine endopeptidases (métabolisme)</term><term>Humains</term><term>Multimérisation de protéines</term><term>Protéines du core viral ()</term><term>Protéines du core viral (métabolisme)</term><term>Protéines virales ()</term><term>Protéines virales (métabolisme)</term><term>Structure tertiaire des protéines</term><term>Virus du SRAS (enzymologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Viral Core Proteins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Viral Core Proteins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cysteine endopeptidases</term><term>Protéines du core viral</term><term>Protéines virales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Crystallography, X-Ray</term><term>Humans</term><term>Protein Conformation</term><term>Protein Multimerization</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Cysteine endopeptidases</term><term>Humains</term><term>Multimérisation de protéines</term><term>Protéines du core viral</term><term>Protéines virales</term><term>Structure tertiaire des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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.</div></front></TEI><affiliations><list><country><li>République populaire de Chine</li></country><region><li>Pékin</li></region><settlement><li>Pékin</li></settlement><orgName><li>Université de Pékin</li></orgName></list><tree><noCountry><name sortKey="Chen, Jiaxuan" sort="Chen, Jiaxuan" uniqKey="Chen J" first="Jiaxuan" last="Chen">Jiaxuan Chen</name><name sortKey="Jin, Changwen" sort="Jin, Changwen" uniqKey="Jin C" first="Changwen" last="Jin">Changwen Jin</name><name sortKey="Kang, Xue" sort="Kang, Xue" uniqKey="Kang X" first="Xue" last="Kang">Xue Kang</name><name sortKey="Liang, Chao" sort="Liang, Chao" uniqKey="Liang C" first="Chao" last="Liang">Chao Liang</name><name sortKey="Lou, Zhiyong" sort="Lou, Zhiyong" uniqKey="Lou Z" first="Zhiyong" last="Lou">Zhiyong Lou</name><name sortKey="Rao, Zihe" sort="Rao, Zihe" uniqKey="Rao Z" first="Zihe" last="Rao">Zihe Rao</name><name sortKey="Xia, Bin" sort="Xia, Bin" uniqKey="Xia B" first="Bin" last="Xia">Bin Xia</name><name sortKey="Xue, Fei" sort="Xue, Fei" uniqKey="Xue F" first="Fei" last="Xue">Fei Xue</name><name sortKey="Zhang, Shengnan" sort="Zhang, Shengnan" uniqKey="Zhang S" first="Shengnan" last="Zhang">Shengnan Zhang</name><name sortKey="Zou, Peng" sort="Zou, Peng" uniqKey="Zou P" first="Peng" last="Zou">Peng Zou</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Zhong, Nan" sort="Zhong, Nan" uniqKey="Zhong N" first="Nan" last="Zhong">Nan Zhong</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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