The dimer interface of the SARS coronavirus nucleocapsid protein adapts a porcine respiratory and reproductive syndrome virus-like structure.
Identifieur interne : 004593 ( Main/Exploration ); précédent : 004592; suivant : 004594The dimer interface of the SARS coronavirus nucleocapsid protein adapts a porcine respiratory and reproductive syndrome virus-like structure.
Auteurs : Chung-Ke Chang [République populaire de Chine] ; Shih-Che Sue ; Tsan-Hung Yu ; Chiu-Min Hsieh ; Cheng-Kun Tsai ; Yen-Chieh Chiang ; Shin-Jye Lee ; Hsin-Hao Hsiao ; Wen-Jin Wu ; Chi-Fon Chang ; Tai-Huang HuangSource :
- FEBS letters [ 0014-5793 ] ; 2005.
Descripteurs français
- KwdFr :
- Alignement de séquences, Animaux, Dimérisation, Données de séquences moléculaires, Liaison hydrogène, Protéines nucléocapside (), Résonance magnétique nucléaire biomoléculaire, Structure secondaire des protéines, Séquence d'acides aminés, Virus du SRAS (), Virus du syndrome respiratoire et reproducteur porcin ().
- MESH :
- Alignement de séquences, Animaux, Dimérisation, Données de séquences moléculaires, Liaison hydrogène, Protéines nucléocapside, Résonance magnétique nucléaire biomoléculaire, Structure secondaire des protéines, Séquence d'acides aminés, Virus du SRAS, Virus du syndrome respiratoire et reproducteur porcin.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Dimerization, Hydrogen Bonding, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Nucleocapsid Proteins (chemistry), Porcine respiratory and reproductive syndrome virus (chemistry), Protein Structure, Secondary, SARS Virus (chemistry), Sequence Alignment.
- MESH :
- chemical , chemistry : Nucleocapsid Proteins.
- chemistry : Porcine respiratory and reproductive syndrome virus, SARS Virus.
- Amino Acid Sequence, Animals, Dimerization, Hydrogen Bonding, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Secondary, Sequence Alignment.
Abstract
We have employed NMR to investigate the structure of SARS coronavirus nucleocapsid protein dimer. We found that the secondary structure of the dimerization domain consists of five alpha helices and a beta-hairpin. The dimer interface consists of a continuous four-stranded beta-sheet superposed by two long alpha helices, reminiscent of that found in the nucleocapsid protein of porcine respiratory and reproductive syndrome virus. Extensive hydrogen bond formation between the two hairpins and hydrophobic interactions between the beta-sheet and the alpha helices render the interface highly stable. Sequence alignment suggests that other coronavirus may share the same structural topology.
DOI: 10.1016/j.febslet.2005.09.038
PubMed: 16214138
Affiliations:
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Le document en format XML
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uniqKey="Sue S" first="Shih-Che" last="Sue">Shih-Che Sue</name></author><author><name sortKey="Yu, Tsan Hung" sort="Yu, Tsan Hung" uniqKey="Yu T" first="Tsan-Hung" last="Yu">Tsan-Hung Yu</name></author><author><name sortKey="Hsieh, Chiu Min" sort="Hsieh, Chiu Min" uniqKey="Hsieh C" first="Chiu-Min" last="Hsieh">Chiu-Min Hsieh</name></author><author><name sortKey="Tsai, Cheng Kun" sort="Tsai, Cheng Kun" uniqKey="Tsai C" first="Cheng-Kun" last="Tsai">Cheng-Kun Tsai</name></author><author><name sortKey="Chiang, Yen Chieh" sort="Chiang, Yen Chieh" uniqKey="Chiang Y" first="Yen-Chieh" last="Chiang">Yen-Chieh Chiang</name></author><author><name sortKey="Lee, Shin Jye" sort="Lee, Shin Jye" uniqKey="Lee S" first="Shin-Jye" last="Lee">Shin-Jye Lee</name></author><author><name sortKey="Hsiao, Hsin Hao" sort="Hsiao, Hsin Hao" uniqKey="Hsiao H" first="Hsin-Hao" last="Hsiao">Hsin-Hao Hsiao</name></author><author><name sortKey="Wu, Wen Jin" sort="Wu, Wen Jin" uniqKey="Wu W" first="Wen-Jin" last="Wu">Wen-Jin Wu</name></author><author><name sortKey="Chang, Chi Fon" sort="Chang, Chi Fon" uniqKey="Chang C" first="Chi-Fon" last="Chang">Chi-Fon Chang</name></author><author><name sortKey="Huang, Tai Huang" sort="Huang, Tai Huang" uniqKey="Huang T" first="Tai-Huang" last="Huang">Tai-Huang Huang</name></author></analytic><series><title level="j">FEBS letters</title><idno type="ISSN">0014-5793</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Dimerization</term><term>Hydrogen Bonding</term><term>Molecular Sequence Data</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Nucleocapsid Proteins (chemistry)</term><term>Porcine respiratory and reproductive syndrome virus (chemistry)</term><term>Protein Structure, Secondary</term><term>SARS Virus (chemistry)</term><term>Sequence 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Resonance, Biomolecular</term><term>Protein Structure, Secondary</term><term>Sequence Alignment</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Animaux</term><term>Dimérisation</term><term>Données de séquences moléculaires</term><term>Liaison hydrogène</term><term>Protéines nucléocapside</term><term>Résonance magnétique nucléaire biomoléculaire</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term><term>Virus du SRAS</term><term>Virus du syndrome respiratoire et reproducteur porcin</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We have employed NMR to investigate the structure of SARS coronavirus nucleocapsid protein dimer. We found that the secondary structure of the dimerization domain consists of five alpha helices and a beta-hairpin. The dimer interface consists of a continuous four-stranded beta-sheet superposed by two long alpha helices, reminiscent of that found in the nucleocapsid protein of porcine respiratory and reproductive syndrome virus. Extensive hydrogen bond formation between the two hairpins and hydrophobic interactions between the beta-sheet and the alpha helices render the interface highly stable. Sequence alignment suggests that other coronavirus may share the same structural topology.</div></front></TEI><affiliations><list><country><li>République populaire de Chine</li></country></list><tree><noCountry><name sortKey="Chang, Chi Fon" sort="Chang, Chi Fon" uniqKey="Chang C" first="Chi-Fon" last="Chang">Chi-Fon Chang</name><name sortKey="Chiang, Yen Chieh" sort="Chiang, Yen Chieh" uniqKey="Chiang Y" first="Yen-Chieh" last="Chiang">Yen-Chieh Chiang</name><name sortKey="Hsiao, Hsin Hao" sort="Hsiao, Hsin Hao" uniqKey="Hsiao H" first="Hsin-Hao" last="Hsiao">Hsin-Hao Hsiao</name><name sortKey="Hsieh, Chiu Min" sort="Hsieh, Chiu Min" uniqKey="Hsieh C" first="Chiu-Min" last="Hsieh">Chiu-Min Hsieh</name><name sortKey="Huang, Tai Huang" sort="Huang, Tai Huang" uniqKey="Huang T" first="Tai-Huang" last="Huang">Tai-Huang Huang</name><name sortKey="Lee, Shin Jye" sort="Lee, Shin Jye" uniqKey="Lee S" first="Shin-Jye" last="Lee">Shin-Jye Lee</name><name sortKey="Sue, Shih Che" sort="Sue, Shih Che" uniqKey="Sue S" first="Shih-Che" last="Sue">Shih-Che Sue</name><name sortKey="Tsai, Cheng Kun" sort="Tsai, Cheng Kun" uniqKey="Tsai C" first="Cheng-Kun" last="Tsai">Cheng-Kun Tsai</name><name sortKey="Wu, Wen Jin" sort="Wu, Wen Jin" uniqKey="Wu W" first="Wen-Jin" last="Wu">Wen-Jin Wu</name><name sortKey="Yu, Tsan Hung" sort="Yu, Tsan Hung" uniqKey="Yu T" first="Tsan-Hung" last="Yu">Tsan-Hung Yu</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Chang, Chung Ke" sort="Chang, Chung Ke" uniqKey="Chang C" first="Chung-Ke" last="Chang">Chung-Ke Chang</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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