A model of the ACE2 structure and function as a SARS-CoV receptor.
Identifieur interne : 005491 ( Main/Exploration ); précédent : 005490; suivant : 005492A model of the ACE2 structure and function as a SARS-CoV receptor.
Auteurs : Ponraj Prabakaran [États-Unis] ; Xiaodong Xiao ; Dimiter S. DimitrovSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 2004.
Descripteurs français
- KwdFr :
- Alignement de séquences (), Analyse de séquence de protéine (), Carboxypeptidases (), Conformation des protéines, Données de séquences moléculaires, Liaison aux protéines, Modèles chimiques, Modèles moléculaires, Peptidyl-Dipeptidase A, Propriétés de surface, Protéines de fusion virale (), Relation structure-activité, Récepteurs viraux (), Simulation numérique, Sites de fixation, Stabilité enzymatique, Séquence d'acides aminés, Virus du SRAS ().
- MESH :
- Alignement de séquences, Analyse de séquence de protéine, Carboxypeptidases, Conformation des protéines, Données de séquences moléculaires, Liaison aux protéines, Modèles chimiques, Modèles moléculaires, Peptidyl-Dipeptidase A, Propriétés de surface, Protéines de fusion virale, Relation structure-activité, Récepteurs viraux, Simulation numérique, Sites de fixation, Stabilité enzymatique, Séquence d'acides aminés, Virus du SRAS.
English descriptors
- KwdEn :
- Amino Acid Sequence, Binding Sites, Carboxypeptidases (chemistry), Computer Simulation, Enzyme Stability, Models, Chemical, Models, Molecular, Molecular Sequence Data, Peptidyl-Dipeptidase A, Protein Binding, Protein Conformation, Receptors, Virus (chemistry), SARS Virus (chemistry), Sequence Alignment (methods), Sequence Analysis, Protein (methods), Structure-Activity Relationship, Surface Properties, Viral Fusion Proteins (chemistry).
- MESH :
- chemical , chemistry : Carboxypeptidases, Receptors, Virus, Viral Fusion Proteins.
- chemistry : SARS Virus.
- methods : Sequence Alignment, Sequence Analysis, Protein.
- Amino Acid Sequence, Binding Sites, Computer Simulation, Enzyme Stability, Models, Chemical, Models, Molecular, Molecular Sequence Data, Peptidyl-Dipeptidase A, Protein Binding, Protein Conformation, Structure-Activity Relationship, Surface Properties.
Abstract
The angiotensin-converting enzyme 2 (ACE2) is an important regulator of the renin-angiotensin system and was very recently identified as a functional receptor for the SARS virus. The ACE2 sequence is similar (sequence identities 43% and 35%, and similarities 61% and 55%, respectively) to those of the testis-specific form of ACE (tACE) and the Drosophila homolog of ACE (AnCE). The high level of sequence similarity allowed us to build a robust homology model of the ACE2 structure with a root-mean-square deviation from the aligned crystal structures of tACE and AnCE less than 0.5A. A prominent feature of the model is a deep channel on the top of the molecule that contains the catalytic site. Negatively charged ridges surrounding the channel may provide a possible binding site for the positively charged receptor-binding domain (RBD) of the S-glycoprotein, which we recently identified [Biochem. Biophys. Res. Commun. 312 (2003) 1159]. Several distinct patches of hydrophobic residues at the ACE2 surface were noted at close proximity to the charged ridges that could contribute to binding. These results suggest a possible binding region for the SARS-CoV S-glycoprotein on ACE2 and could help in the design of experiments to further elucidate the structure and function of ACE2.
DOI: 10.1016/j.bbrc.2003.12.081
PubMed: 14715271
Affiliations:
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Dimitrov</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="ISSN">0006-291X</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>Binding Sites</term><term>Carboxypeptidases (chemistry)</term><term>Computer Simulation</term><term>Enzyme Stability</term><term>Models, Chemical</term><term>Models, Molecular</term><term>Molecular Sequence Data</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>Sequence Alignment (methods)</term><term>Sequence Analysis, Protein (methods)</term><term>Structure-Activity Relationship</term><term>Surface Properties</term><term>Viral Fusion Proteins (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences ()</term><term>Analyse de séquence de protéine ()</term><term>Carboxypeptidases ()</term><term>Conformation des protéines</term><term>Données de séquences moléculaires</term><term>Liaison aux protéines</term><term>Modèles chimiques</term><term>Modèles moléculaires</term><term>Peptidyl-Dipeptidase A</term><term>Propriétés de surface</term><term>Protéines de fusion virale ()</term><term>Relation structure-activité</term><term>Récepteurs viraux ()</term><term>Simulation numérique</term><term>Sites de fixation</term><term>Stabilité enzymatique</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 Fusion Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Sequence Alignment</term><term>Sequence Analysis, Protein</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Binding Sites</term><term>Computer Simulation</term><term>Enzyme Stability</term><term>Models, Chemical</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Peptidyl-Dipeptidase A</term><term>Protein Binding</term><term>Protein Conformation</term><term>Structure-Activity Relationship</term><term>Surface Properties</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Analyse de séquence de protéine</term><term>Carboxypeptidases</term><term>Conformation des protéines</term><term>Données de séquences moléculaires</term><term>Liaison aux protéines</term><term>Modèles chimiques</term><term>Modèles moléculaires</term><term>Peptidyl-Dipeptidase A</term><term>Propriétés de surface</term><term>Protéines de fusion virale</term><term>Relation structure-activité</term><term>Récepteurs viraux</term><term>Simulation numérique</term><term>Sites de fixation</term><term>Stabilité enzymatique</term><term>Séquence d'acides aminés</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The angiotensin-converting enzyme 2 (ACE2) is an important regulator of the renin-angiotensin system and was very recently identified as a functional receptor for the SARS virus. The ACE2 sequence is similar (sequence identities 43% and 35%, and similarities 61% and 55%, respectively) to those of the testis-specific form of ACE (tACE) and the Drosophila homolog of ACE (AnCE). The high level of sequence similarity allowed us to build a robust homology model of the ACE2 structure with a root-mean-square deviation from the aligned crystal structures of tACE and AnCE less than 0.5A. A prominent feature of the model is a deep channel on the top of the molecule that contains the catalytic site. Negatively charged ridges surrounding the channel may provide a possible binding site for the positively charged receptor-binding domain (RBD) of the S-glycoprotein, which we recently identified [Biochem. Biophys. Res. Commun. 312 (2003) 1159]. Several distinct patches of hydrophobic residues at the ACE2 surface were noted at close proximity to the charged ridges that could contribute to binding. These results suggest a possible binding region for the SARS-CoV S-glycoprotein on ACE2 and could help in the design of experiments to further elucidate the structure and function of ACE2.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Maryland</li></region></list><tree><noCountry><name sortKey="Dimitrov, Dimiter S" sort="Dimitrov, Dimiter S" uniqKey="Dimitrov D" first="Dimiter S" last="Dimitrov">Dimiter S. Dimitrov</name><name sortKey="Xiao, Xiaodong" sort="Xiao, Xiaodong" uniqKey="Xiao X" first="Xiaodong" last="Xiao">Xiaodong Xiao</name></noCountry><country name="États-Unis"><region name="Maryland"><name sortKey="Prabakaran, Ponraj" sort="Prabakaran, Ponraj" uniqKey="Prabakaran P" first="Ponraj" last="Prabakaran">Ponraj Prabakaran</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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