SrasV1, Main, Exploration, bibRecord, 005358

Exploring the binding mechanism of the main proteinase in SARS-associated coronavirus and its implication to anti-SARS drug design.

Identifieur interne : 005358 ( Main/Exploration ); précédent : 005357; suivant : 005359

Exploring 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 Yap

Source :

Bioorganic & medicinal chemistry [ 0968-0896 ] ; 2004.

RBID : pubmed:15080921

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

Affiliations:

République populaire de Chine

Le document en format XML

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<term>Protéines virales (métabolisme)</term>
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<term>Séquence d'acides aminés</term>
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<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
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<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>
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Serveur d'exploration SRAS

Exploring the binding mechanism of the main proteinase in SARS-associated coronavirus and its implication to anti-SARS drug design.

Exploring the binding mechanism of the main proteinase in SARS-associated coronavirus and its implication to anti-SARS drug design.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki

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