Exploring the binding mechanism of the main proteinase in SARS-associated coronavirus and its implication to anti-SARS drug design.
Identifieur interne : 005358 ( Main/Curation ); précédent : 005357; suivant : 005359Exploring the binding mechanism of the main proteinase in SARS-associated coronavirus and its implication to anti-SARS drug design.
Auteurs : Xue Wu Zhang [République populaire de Chine] ; Yee Leng YapSource :
- Bioorganic & medicinal chemistry [ 0968-0896 ] ; 2004.
Descripteurs français
- KwdFr :
- Antiviraux (), Antiviraux (métabolisme), Antiviraux (pharmacologie), Conception de médicament, Cysteine endopeptidases, Données de séquences moléculaires, Endopeptidases (), Endopeptidases (métabolisme), Liaison aux protéines, Modèles moléculaires, Protéines virales (), Protéines virales (métabolisme), Similitude de séquences d'acides aminés, Séquence d'acides aminés.
- MESH :
- métabolisme : Antiviraux, Endopeptidases, Protéines virales.
- pharmacologie : Antiviraux.
- Antiviraux, Conception de médicament, Cysteine endopeptidases, Données de séquences moléculaires, Endopeptidases, Liaison aux protéines, Modèles moléculaires, Protéines virales, Similitude de séquences d'acides aminés, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Antiviral Agents (chemistry), Antiviral Agents (metabolism), Antiviral Agents (pharmacology), Cysteine Endopeptidases, Drug Design, Endopeptidases (chemistry), Endopeptidases (metabolism), Models, Molecular, Molecular Sequence Data, Protein Binding, Sequence Homology, Amino Acid, Viral Proteins (chemistry), Viral Proteins (metabolism).
- MESH :
- chemical , chemistry : Antiviral Agents, Endopeptidases, Viral Proteins.
- chemical , metabolism : Antiviral Agents, Endopeptidases, Viral Proteins.
- chemical , pharmacology : Antiviral Agents.
- Amino Acid Sequence, Cysteine Endopeptidases, Drug Design, Models, Molecular, Molecular Sequence Data, Protein Binding, Sequence Homology, Amino Acid.
Abstract
The main proteinase of SARS-associated coronavirus (SARS-CoV) plays an important role in viral transcription and replication, and is an attractive target for anti-SARS drug development. The important thing is to understand its binding mechanism with possible ligands. In this study, we investigated possible noncanonical interactions, potential inhibitors, and binding pockets in the main proteinase of SARS-CoV based on its recently determined crystal structure. These findings provide a wide clue to searching for anti-SARS drug. Interestingly, we found that similar structure patterns exist in SARS-CoV main proteinase with Poliovirus 3c Proteinase, Rhinovirus 3c Protease, Nsp4 Proteinase From Equine Arteritis Virus, Hepatitis C Virus Ns3 Protease, Hepatitis A Virus 3c Protease, and Dengue Virus Ns3 Protease. It suggests that the available drugs in these viruses could be used to fight SARS disease.
DOI: 10.1016/j.bmc.2004.02.015
PubMed: 15080921
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: Pour aller vers cette notice dans l'étape Curation :002E53
- to stream PubMed, to step Curation: Pour aller vers cette notice dans l'étape Curation :002E53
- to stream PubMed, to step Checkpoint: Pour aller vers cette notice dans l'étape Curation :002D08
- to stream Ncbi, to step Merge: Pour aller vers cette notice dans l'étape Curation :000748
- to stream Ncbi, to step Curation: Pour aller vers cette notice dans l'étape Curation :000748
- to stream Ncbi, to step Checkpoint: Pour aller vers cette notice dans l'étape Curation :000748
- to stream Main, to step Merge: Pour aller vers cette notice dans l'étape Curation :005776
Links to Exploration step
pubmed:15080921Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Exploring the binding mechanism of the main proteinase in SARS-associated coronavirus and its implication to anti-SARS drug design.</title>
<author><name sortKey="Zhang, Xue Wu" sort="Zhang, Xue Wu" uniqKey="Zhang X" first="Xue Wu" last="Zhang">Xue Wu Zhang</name>
<affiliation wicri:level="1"><nlm:affiliation>HKU-Pasteur Research Center, Bioinformatics, 8 Sassoon Road, Hong Kong, China. xwzhang@hkucc.hku.hk</nlm:affiliation>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>HKU-Pasteur Research Center, Bioinformatics, 8 Sassoon Road, Hong Kong</wicri:regionArea>
<wicri:noRegion>Hong Kong</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Yap, Yee Leng" sort="Yap, Yee Leng" uniqKey="Yap Y" first="Yee Leng" last="Yap">Yee Leng Yap</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2004">2004</date>
<idno type="RBID">pubmed:15080921</idno>
<idno type="pmid">15080921</idno>
<idno type="doi">10.1016/j.bmc.2004.02.015</idno>
<idno type="wicri:Area/PubMed/Corpus">002E53</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002E53</idno>
<idno type="wicri:Area/PubMed/Curation">002E53</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002E53</idno>
<idno type="wicri:Area/PubMed/Checkpoint">002D08</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002D08</idno>
<idno type="wicri:Area/Ncbi/Merge">000748</idno>
<idno type="wicri:Area/Ncbi/Curation">000748</idno>
<idno type="wicri:Area/Ncbi/Checkpoint">000748</idno>
<idno type="wicri:doubleKey">0968-0896:2004:Zhang X:exploring:the:binding</idno>
<idno type="wicri:Area/Main/Merge">005776</idno>
<idno type="wicri:Area/Main/Curation">005358</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Exploring the binding mechanism of the main proteinase in SARS-associated coronavirus and its implication to anti-SARS drug design.</title>
<author><name sortKey="Zhang, Xue Wu" sort="Zhang, Xue Wu" uniqKey="Zhang X" first="Xue Wu" last="Zhang">Xue Wu Zhang</name>
<affiliation wicri:level="1"><nlm:affiliation>HKU-Pasteur Research Center, Bioinformatics, 8 Sassoon Road, Hong Kong, China. xwzhang@hkucc.hku.hk</nlm:affiliation>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>HKU-Pasteur Research Center, Bioinformatics, 8 Sassoon Road, Hong Kong</wicri:regionArea>
<wicri:noRegion>Hong Kong</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Yap, Yee Leng" sort="Yap, Yee Leng" uniqKey="Yap Y" first="Yee Leng" last="Yap">Yee Leng Yap</name>
</author>
</analytic>
<series><title level="j">Bioorganic & medicinal chemistry</title>
<idno type="ISSN">0968-0896</idno>
<imprint><date when="2004" type="published">2004</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Antiviral Agents (chemistry)</term>
<term>Antiviral Agents (metabolism)</term>
<term>Antiviral Agents (pharmacology)</term>
<term>Cysteine Endopeptidases</term>
<term>Drug Design</term>
<term>Endopeptidases (chemistry)</term>
<term>Endopeptidases (metabolism)</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>Sequence Homology, Amino Acid</term>
<term>Viral Proteins (chemistry)</term>
<term>Viral Proteins (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Antiviraux ()</term>
<term>Antiviraux (métabolisme)</term>
<term>Antiviraux (pharmacologie)</term>
<term>Conception de médicament</term>
<term>Cysteine endopeptidases</term>
<term>Données de séquences moléculaires</term>
<term>Endopeptidases ()</term>
<term>Endopeptidases (métabolisme)</term>
<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
<term>Protéines virales ()</term>
<term>Protéines virales (métabolisme)</term>
<term>Similitude de séquences d'acides aminés</term>
<term>Séquence d'acides aminés</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antiviral Agents</term>
<term>Endopeptidases</term>
<term>Viral Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antiviral Agents</term>
<term>Endopeptidases</term>
<term>Viral Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antiviral Agents</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Antiviraux</term>
<term>Endopeptidases</term>
<term>Protéines virales</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antiviraux</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Cysteine Endopeptidases</term>
<term>Drug Design</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>Sequence Homology, Amino Acid</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Antiviraux</term>
<term>Conception de médicament</term>
<term>Cysteine endopeptidases</term>
<term>Données de séquences moléculaires</term>
<term>Endopeptidases</term>
<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
<term>Protéines virales</term>
<term>Similitude de séquences d'acides aminés</term>
<term>Séquence d'acides aminés</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">The main proteinase of SARS-associated coronavirus (SARS-CoV) plays an important role in viral transcription and replication, and is an attractive target for anti-SARS drug development. The important thing is to understand its binding mechanism with possible ligands. In this study, we investigated possible noncanonical interactions, potential inhibitors, and binding pockets in the main proteinase of SARS-CoV based on its recently determined crystal structure. These findings provide a wide clue to searching for anti-SARS drug. Interestingly, we found that similar structure patterns exist in SARS-CoV main proteinase with Poliovirus 3c Proteinase, Rhinovirus 3c Protease, Nsp4 Proteinase From Equine Arteritis Virus, Hepatitis C Virus Ns3 Protease, Hepatitis A Virus 3c Protease, and Dengue Virus Ns3 Protease. It suggests that the available drugs in these viruses could be used to fight SARS disease.</div>
</front>
</TEI>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/Main/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 005358 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Curation/biblio.hfd -nk 005358 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= SrasV1 |flux= Main |étape= Curation |type= RBID |clé= pubmed:15080921 |texte= Exploring the binding mechanism of the main proteinase in SARS-associated coronavirus and its implication to anti-SARS drug design. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Curation/RBID.i -Sk "pubmed:15080921" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Curation/biblio.hfd \ | NlmPubMed2Wicri -a SrasV1
![]() | This area was generated with Dilib version V0.6.33. | ![]() |