A molecular docking model of SARS-CoV S1 protein in complex with its receptor, human ACE2.
Identifieur interne : 004949 ( Main/Exploration ); précédent : 004948; suivant : 004950A molecular docking model of SARS-CoV S1 protein in complex with its receptor, human ACE2.
Auteurs : Yuan Zhang [République populaire de Chine] ; Nan Zheng ; Pei Hao ; Ying Cao ; Yang ZhongSource :
- Computational biology and chemistry [ 1476-9271 ] ; 2005.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- 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
Affiliations:
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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></author></analytic><series><title level="j">Computational biology and chemistry</title><idno type="ISSN">1476-9271</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>Binding Sites</term><term>Carboxypeptidases (chemistry)</term><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><term>Viral Proteins (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Carboxypeptidases ()</term><term>Conformation des protéines</term><term>Humains</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Peptidyl-Dipeptidase A</term><term>Protéines virales ()</term><term>Récepteurs viraux ()</term><term>Sites de fixation</term><term>Séquence d'acides aminés</term><term>Virus du SRAS ()</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Carboxypeptidases</term><term>Receptors, Virus</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Binding Sites</term><term>Humans</term><term>Models, Molecular</term><term>Peptidyl-Dipeptidase A</term><term>Protein Binding</term><term>Protein Conformation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Carboxypeptidases</term><term>Conformation des protéines</term><term>Humains</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Peptidyl-Dipeptidase A</term><term>Protéines virales</term><term>Récepteurs viraux</term><term>Sites de fixation</term><term>Séquence d'acides aminés</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><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></front></TEI><affiliations><list><country><li>République populaire de Chine</li></country></list><tree><noCountry><name sortKey="Cao, Ying" sort="Cao, Ying" uniqKey="Cao Y" first="Ying" last="Cao">Ying Cao</name><name sortKey="Hao, Pei" sort="Hao, Pei" uniqKey="Hao P" first="Pei" last="Hao">Pei Hao</name><name sortKey="Zheng, Nan" sort="Zheng, Nan" uniqKey="Zheng N" first="Nan" last="Zheng">Nan Zheng</name><name sortKey="Zhong, Yang" sort="Zhong, Yang" uniqKey="Zhong Y" first="Yang" last="Zhong">Yang Zhong</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Zhang, Yuan" sort="Zhang, Yuan" uniqKey="Zhang Y" first="Yuan" last="Zhang">Yuan Zhang</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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