Structural basis for the recognition of the SARS-CoV-2 by full-length human ACE2.
Identifieur interne : 000170 ( an2020/Analysis ); précédent : 000169; suivant : 000171Structural basis for the recognition of the SARS-CoV-2 by full-length human ACE2.
Auteurs : Renhong Yan [République populaire de Chine] ; Yuanyuan Zhang [République populaire de Chine] ; Yaning Li [République populaire de Chine] ; Lu Xia [République populaire de Chine] ; Yingying Guo [République populaire de Chine] ; Qiang Zhou [République populaire de Chine]Source :
- Science (New York, N.Y.) [ 1095-9203 ] ; 2020.
Abstract
Angiotensin-converting enzyme 2 (ACE2) is the cellular receptor for SARS coronavirus (SARS-CoV) and the new coronavirus (SARS-CoV-2) that is causing the serious epidemic COVID-19. Here we present cryo-EM structures of full-length human ACE2, in the presence of a neutral amino acid transporter B0AT1, with or without the receptor binding domain (RBD) of the surface spike glycoprotein (S protein) of SARS-CoV-2, both at an overall resolution of 2.9 Å, with a local resolution of 3.5 Å at the ACE2-RBD interface. The ACE2-B0AT1 complex is assembled as a dimer of heterodimers, with the Collectrin-like domain (CLD) of ACE2 mediating homo-dimerization. The RBD is recognized by the extracellular peptidase domain (PD) of ACE2 mainly through polar residues. These findings provide important insights to the molecular basis for coronavirus recognition and infection.
DOI: 10.1126/science.abb2762
PubMed: 32132184
Affiliations:
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Province</wicri:noRegion></affiliation></author></analytic><series><title level="j">Science (New York, N.Y.)</title><idno type="eISSN">1095-9203</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Angiotensin-converting enzyme 2 (ACE2) is the cellular receptor for SARS coronavirus (SARS-CoV) and the new coronavirus (SARS-CoV-2) that is causing the serious epidemic COVID-19. Here we present cryo-EM structures of full-length human ACE2, in the presence of a neutral amino acid transporter B<sup>0</sup>AT1, with or without the receptor binding domain (RBD) of the surface spike glycoprotein (S protein) of SARS-CoV-2, both at an overall resolution of 2.9 Å, with a local resolution of 3.5 Å at the ACE2-RBD interface. The ACE2-B<sup>0</sup>AT1 complex is assembled as a dimer of heterodimers, with the Collectrin-like domain (CLD) of ACE2 mediating homo-dimerization. The RBD is recognized by the extracellular peptidase domain (PD) of ACE2 mainly through polar residues. These findings provide important insights to the molecular basis for coronavirus recognition and infection.</div></front></TEI><affiliations><list><country><li>République populaire de Chine</li></country><settlement><li>Pékin</li></settlement></list><tree><country name="République populaire de Chine"><noRegion><name sortKey="Yan, Renhong" sort="Yan, Renhong" uniqKey="Yan R" first="Renhong" last="Yan">Renhong Yan</name></noRegion><name sortKey="Guo, Yingying" sort="Guo, Yingying" uniqKey="Guo Y" first="Yingying" last="Guo">Yingying Guo</name><name sortKey="Li, Yaning" sort="Li, Yaning" uniqKey="Li Y" first="Yaning" last="Li">Yaning Li</name><name sortKey="Xia, Lu" sort="Xia, Lu" uniqKey="Xia L" first="Lu" last="Xia">Lu Xia</name><name sortKey="Zhang, Yuanyuan" sort="Zhang, Yuanyuan" uniqKey="Zhang Y" first="Yuanyuan" last="Zhang">Yuanyuan Zhang</name><name sortKey="Zhou, Qiang" sort="Zhou, Qiang" uniqKey="Zhou Q" first="Qiang" last="Zhou">Qiang Zhou</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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