SrasV1, PubMed, Checkpoint, bibRecord, 002E62

A model of the ACE2 structure and function as a SARS-CoV receptor.

Identifieur interne : 002E62 ( PubMed/Checkpoint ); précédent : 002E61; suivant : 002E63

A model of the ACE2 structure and function as a SARS-CoV receptor.

Auteurs : Ponraj Prabakaran [États-Unis] ; Xiaodong Xiao ; Dimiter S. Dimitrov

Source :

Biochemical and biophysical research communications [ 0006-291X ] ; 2004.

RBID : pubmed:14715271

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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Le document en format XML

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<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>
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<ReferenceList><Reference><Citation>J Mol Biol. 1971 Feb 14;55(3):379-400</Citation>
<ArticleIdList><ArticleId IdType="pubmed">5551392</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Brief Bioinform. 2002 Sep;3(3):265-74</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12230035</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 2003 Dec 26;312(4):1159-64</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14651994</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Mol Biol. 1982 May 5;157(1):105-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7108955</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Nature. 2002 Jun 20;417(6891):822-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12075344</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 2003 Oct 10;310(1):78-83</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14511651</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Nat Rev Microbiol. 2004 Feb;2(2):109-22</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15043007</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Protein Sci. 1998 Jun;7(6):1431-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9655348</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Proteins. 1991;11(4):281-96</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1758883</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Nature. 2003 Nov 27;426(6965):450-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14647384</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Protein Eng. 1987 Oct-Nov;1(5):385-92</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3508287</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Cell. 2000 Jun 23;101(7):697-702</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10892741</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Circ Res. 2000 Sep 1;87(5):E1-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10969042</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Biol Chem. 2000 Oct 27;275(43):33238-43</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10924499</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Biochemistry. 2003 Nov 18;42(45):13185-92</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14609329</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Protein Eng. 1987 Oct-Nov;1(5):377-84</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3508286</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>FEBS Lett. 2003 Mar 13;538(1-3):65-70</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12633854</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Nature. 2003 Jan 30;421(6922):551-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12540854</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Nucleic Acids Res. 1994 Nov 11;22(22):4673-80</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7984417</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
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</country>
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</region>
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A model of the ACE2 structure and function as a SARS-CoV receptor.

A model of the ACE2 structure and function as a SARS-CoV receptor.

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Descripteurs français

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Abstract

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