SrasV1, PubMed, Corpus, bibRecord, 002670

A molecular docking model of SARS-CoV S1 protein in complex with its receptor, human ACE2.

Identifieur interne : 002670 ( PubMed/Corpus ); précédent : 002669; suivant : 002671

A molecular docking model of SARS-CoV S1 protein in complex with its receptor, human ACE2.

Auteurs : Yuan Zhang ; Nan Zheng ; Pei Hao ; Ying Cao ; Yang Zhong

Source :

Computational biology and chemistry [ 1476-9271 ] ; 2005.

RBID : pubmed:15979045

English descriptors

KwdEn :
- Amino Acid Sequence, Binding Sites, Carboxypeptidases (chemistry), Humans, Models, Molecular, Peptidyl-Dipeptidase A, Protein Binding, Protein Conformation, Receptors, Virus (chemistry), SARS Virus (chemistry), Viral Proteins (chemistry).
MESH :
- chemical , chemistry : Carboxypeptidases, Receptors, Virus, Viral Proteins.
- chemistry : SARS Virus.
- Amino Acid Sequence, Binding Sites, Humans, Models, Molecular, Peptidyl-Dipeptidase A, Protein Binding, Protein Conformation.

Abstract

The exact residues within severe acute respiratory syndrome coronavirus (SARS-CoV) S1 protein and its receptor, human ACE2, involved in their interaction still remain largely undetermined. Identification of exact amino acid residues that are crucial for the interaction of S1 with ACE2 could provide working hypotheses for experimental studies and might be helpful for the development of antiviral inhibitor. In this paper, a molecular docking model of SARS-CoV S1 protein in complex with human ACE2 was constructed. The interacting residue pairs within this complex model and their contact types were also identified. Our model, supported by significant biochemical evidence, suggested receptor-binding residues were concentrated in two segments of S1 protein. In contrast, the interfacial residues in ACE2, though close to each other in tertiary structure, were found to be widely scattered in the primary sequence. In particular, the S1 residue ARG453 and ACE2 residue LYS341 might be the key residues in the complex formation.

DOI: 10.1016/j.compbiolchem.2005.04.008
PubMed: 15979045

Links to Exploration step

pubmed:15979045

Le document en format XML

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<author><name sortKey="Zhang, Yuan" sort="Zhang, Yuan" uniqKey="Zhang Y" first="Yuan" last="Zhang">Yuan Zhang</name>
<affiliation><nlm:affiliation>School of Life Sciences, Fudan University, Shanghai 200433, China.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Zheng, Nan" sort="Zheng, Nan" uniqKey="Zheng N" first="Nan" last="Zheng">Nan Zheng</name>
</author>
<author><name sortKey="Hao, Pei" sort="Hao, Pei" uniqKey="Hao P" first="Pei" last="Hao">Pei Hao</name>
</author>
<author><name sortKey="Cao, Ying" sort="Cao, Ying" uniqKey="Cao Y" first="Ying" last="Cao">Ying Cao</name>
</author>
<author><name sortKey="Zhong, Yang" sort="Zhong, Yang" uniqKey="Zhong Y" first="Yang" last="Zhong">Yang Zhong</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">A molecular docking model of SARS-CoV S1 protein in complex with its receptor, human ACE2.</title>
<author><name sortKey="Zhang, Yuan" sort="Zhang, Yuan" uniqKey="Zhang Y" first="Yuan" last="Zhang">Yuan Zhang</name>
<affiliation><nlm:affiliation>School of Life Sciences, Fudan University, Shanghai 200433, China.</nlm:affiliation>
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<author><name sortKey="Zheng, Nan" sort="Zheng, Nan" uniqKey="Zheng N" first="Nan" last="Zheng">Nan Zheng</name>
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<author><name sortKey="Hao, Pei" sort="Hao, Pei" uniqKey="Hao P" first="Pei" last="Hao">Pei Hao</name>
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<author><name sortKey="Cao, Ying" sort="Cao, Ying" uniqKey="Cao Y" first="Ying" last="Cao">Ying Cao</name>
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<author><name sortKey="Zhong, Yang" sort="Zhong, Yang" uniqKey="Zhong Y" first="Yang" last="Zhong">Yang Zhong</name>
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<term>Humans</term>
<term>Models, Molecular</term>
<term>Peptidyl-Dipeptidase A</term>
<term>Protein Binding</term>
<term>Protein Conformation</term>
<term>Receptors, Virus (chemistry)</term>
<term>SARS Virus (chemistry)</term>
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<front><div type="abstract" xml:lang="en">The exact residues within severe acute respiratory syndrome coronavirus (SARS-CoV) S1 protein and its receptor, human ACE2, involved in their interaction still remain largely undetermined. Identification of exact amino acid residues that are crucial for the interaction of S1 with ACE2 could provide working hypotheses for experimental studies and might be helpful for the development of antiviral inhibitor. In this paper, a molecular docking model of SARS-CoV S1 protein in complex with human ACE2 was constructed. The interacting residue pairs within this complex model and their contact types were also identified. Our model, supported by significant biochemical evidence, suggested receptor-binding residues were concentrated in two segments of S1 protein. In contrast, the interfacial residues in ACE2, though close to each other in tertiary structure, were found to be widely scattered in the primary sequence. In particular, the S1 residue ARG453 and ACE2 residue LYS341 might be the key residues in the complex formation.</div>
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<Abstract><AbstractText>The exact residues within severe acute respiratory syndrome coronavirus (SARS-CoV) S1 protein and its receptor, human ACE2, involved in their interaction still remain largely undetermined. Identification of exact amino acid residues that are crucial for the interaction of S1 with ACE2 could provide working hypotheses for experimental studies and might be helpful for the development of antiviral inhibitor. In this paper, a molecular docking model of SARS-CoV S1 protein in complex with human ACE2 was constructed. The interacting residue pairs within this complex model and their contact types were also identified. Our model, supported by significant biochemical evidence, suggested receptor-binding residues were concentrated in two segments of S1 protein. In contrast, the interfacial residues in ACE2, though close to each other in tertiary structure, were found to be widely scattered in the primary sequence. In particular, the S1 residue ARG453 and ACE2 residue LYS341 might be the key residues in the complex formation.</AbstractText>
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A molecular docking model of SARS-CoV S1 protein in complex with its receptor, human ACE2.

A molecular docking model of SARS-CoV S1 protein in complex with its receptor, human ACE2.

Source :

English descriptors

Abstract

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

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