Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2.
Identifieur interne : 000697 ( PubMed/Corpus ); précédent : 000696; suivant : 000698Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2.
Auteurs : Renhong Yan ; Yuanyuan Zhang ; Yaning Li ; Lu Xia ; Yingying Guo ; Qiang ZhouSource :
- Science (New York, N.Y.) [ 1095-9203 ] ; 2020.
English descriptors
- KwdEn :
- Amino Acid Sequence, Amino Acid Transport Systems, Neutral (ultrastructure), Betacoronavirus, Coronavirus Infections, Cryoelectron Microscopy, Humans, Models, Molecular, Pandemics, Peptidyl-Dipeptidase A (ultrastructure), Pneumonia, Viral, Protein Binding, Protein Domains, Protein Multimerization, Receptors, Virus (ultrastructure), SARS Virus, Sequence Alignment, Spike Glycoprotein, Coronavirus (ultrastructure).
- MESH :
- chemical , ultrastructure : Amino Acid Transport Systems, Neutral, Peptidyl-Dipeptidase A, Receptors, Virus, Spike Glycoprotein, Coronavirus.
- Amino Acid Sequence, Betacoronavirus, Coronavirus Infections, Cryoelectron Microscopy, Humans, Models, Molecular, Pandemics, Pneumonia, Viral, Protein Binding, Protein Domains, Protein Multimerization, SARS Virus, Sequence Alignment.
Abstract
Angiotensin-converting enzyme 2 (ACE2) is the cellular receptor for severe acute respiratory syndrome-coronavirus (SARS-CoV) and the new coronavirus (SARS-CoV-2) that is causing the serious coronavirus disease 2019 (COVID-19) epidemic. Here, we present cryo-electron microscopy structures of full-length human ACE2 in the presence of the 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 angstroms, with a local resolution of 3.5 angstroms at the ACE2-RBD interface. The ACE2-B0AT1 complex is assembled as a dimer of heterodimers, with the collectrin-like domain of ACE2 mediating homodimerization. The RBD is recognized by the extracellular peptidase domain of ACE2 mainly through polar residues. These findings provide important insights into the molecular basis for coronavirus recognition and infection.
DOI: 10.1126/science.abb2762
PubMed: 32132184
Links to Exploration step
pubmed:32132184Le document en format XML
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last="Li">Yaning Li</name><affiliation><nlm:affiliation>Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.</nlm:affiliation></affiliation></author><author><name sortKey="Xia, Lu" sort="Xia, Lu" uniqKey="Xia L" first="Lu" last="Xia">Lu Xia</name><affiliation><nlm:affiliation>Key Laboratory of Structural Biology of Zhejiang Province, Institute of Biology, Westlake Institute for Advanced Study, 18 Shilongshan Road, Hangzhou 310024, Zhejiang Province, China.</nlm:affiliation></affiliation></author><author><name sortKey="Guo, Yingying" sort="Guo, Yingying" uniqKey="Guo Y" first="Yingying" last="Guo">Yingying Guo</name><affiliation><nlm:affiliation>Key Laboratory of Structural Biology of Zhejiang Province, Institute of Biology, Westlake Institute for Advanced Study, 18 Shilongshan Road, Hangzhou 310024, Zhejiang Province, China.</nlm:affiliation></affiliation></author><author><name sortKey="Zhou, Qiang" sort="Zhou, Qiang" uniqKey="Zhou Q" first="Qiang" last="Zhou">Qiang Zhou</name><affiliation><nlm:affiliation>Key Laboratory of Structural Biology of Zhejiang Province, Institute of Biology, Westlake Institute for Advanced Study, 18 Shilongshan Road, Hangzhou 310024, Zhejiang Province, China. zhouqiang@westlake.edu.cn.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2020">2020</date><idno type="RBID">pubmed:32132184</idno><idno type="pmid">32132184</idno><idno type="doi">10.1126/science.abb2762</idno><idno type="wicri:Area/PubMed/Corpus">000697</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000697</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2.</title><author><name sortKey="Yan, Renhong" sort="Yan, Renhong" uniqKey="Yan R" first="Renhong" last="Yan">Renhong Yan</name><affiliation><nlm:affiliation>Key Laboratory of Structural Biology of Zhejiang Province, Institute of Biology, Westlake Institute for Advanced Study, 18 Shilongshan Road, Hangzhou 310024, Zhejiang Province, China.</nlm:affiliation></affiliation></author><author><name sortKey="Zhang, Yuanyuan" sort="Zhang, Yuanyuan" uniqKey="Zhang Y" first="Yuanyuan" last="Zhang">Yuanyuan Zhang</name><affiliation><nlm:affiliation>Key Laboratory of Structural Biology of Zhejiang Province, Institute of Biology, Westlake Institute for Advanced Study, 18 Shilongshan Road, Hangzhou 310024, Zhejiang Province, China.</nlm:affiliation></affiliation></author><author><name sortKey="Li, Yaning" sort="Li, Yaning" uniqKey="Li Y" first="Yaning" last="Li">Yaning Li</name><affiliation><nlm:affiliation>Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.</nlm:affiliation></affiliation></author><author><name sortKey="Xia, Lu" sort="Xia, Lu" uniqKey="Xia L" first="Lu" last="Xia">Lu Xia</name><affiliation><nlm:affiliation>Key Laboratory of Structural Biology of Zhejiang Province, Institute of Biology, Westlake Institute for Advanced Study, 18 Shilongshan Road, Hangzhou 310024, Zhejiang Province, China.</nlm:affiliation></affiliation></author><author><name sortKey="Guo, Yingying" sort="Guo, Yingying" uniqKey="Guo Y" first="Yingying" last="Guo">Yingying Guo</name><affiliation><nlm:affiliation>Key Laboratory of Structural Biology of Zhejiang Province, Institute of Biology, Westlake Institute for Advanced Study, 18 Shilongshan Road, Hangzhou 310024, Zhejiang Province, China.</nlm:affiliation></affiliation></author><author><name sortKey="Zhou, Qiang" sort="Zhou, Qiang" uniqKey="Zhou Q" first="Qiang" last="Zhou">Qiang Zhou</name><affiliation><nlm:affiliation>Key Laboratory of Structural Biology of Zhejiang Province, Institute of Biology, Westlake Institute for Advanced Study, 18 Shilongshan Road, Hangzhou 310024, Zhejiang Province, China. zhouqiang@westlake.edu.cn.</nlm:affiliation></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><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Amino Acid Transport Systems, Neutral (ultrastructure)</term><term>Betacoronavirus</term><term>Coronavirus Infections</term><term>Cryoelectron Microscopy</term><term>Humans</term><term>Models, Molecular</term><term>Pandemics</term><term>Peptidyl-Dipeptidase A (ultrastructure)</term><term>Pneumonia, Viral</term><term>Protein Binding</term><term>Protein Domains</term><term>Protein Multimerization</term><term>Receptors, Virus (ultrastructure)</term><term>SARS Virus</term><term>Sequence Alignment</term><term>Spike Glycoprotein, Coronavirus (ultrastructure)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Amino Acid Transport Systems, Neutral</term><term>Peptidyl-Dipeptidase A</term><term>Receptors, Virus</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Betacoronavirus</term><term>Coronavirus Infections</term><term>Cryoelectron Microscopy</term><term>Humans</term><term>Models, Molecular</term><term>Pandemics</term><term>Pneumonia, Viral</term><term>Protein Binding</term><term>Protein Domains</term><term>Protein Multimerization</term><term>SARS Virus</term><term>Sequence Alignment</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Angiotensin-converting enzyme 2 (ACE2) is the cellular receptor for severe acute respiratory syndrome-coronavirus (SARS-CoV) and the new coronavirus (SARS-CoV-2) that is causing the serious coronavirus disease 2019 (COVID-19) epidemic. Here, we present cryo-electron microscopy structures of full-length human ACE2 in the presence of the 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 angstroms, with a local resolution of 3.5 angstroms 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 of ACE2 mediating homodimerization. The RBD is recognized by the extracellular peptidase domain of ACE2 mainly through polar residues. These findings provide important insights into the molecular basis for coronavirus recognition and infection.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">32132184</PMID><DateCompleted><Year>2020</Year><Month>04</Month><Day>01</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>01</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1095-9203</ISSN><JournalIssue CitedMedium="Internet"><Volume>367</Volume><Issue>6485</Issue><PubDate><Year>2020</Year><Month>03</Month><Day>27</Day></PubDate></JournalIssue><Title>Science (New York, N.Y.)</Title><ISOAbbreviation>Science</ISOAbbreviation></Journal><ArticleTitle>Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2.</ArticleTitle><Pagination><MedlinePgn>1444-1448</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1126/science.abb2762</ELocationID><Abstract><AbstractText>Angiotensin-converting enzyme 2 (ACE2) is the cellular receptor for severe acute respiratory syndrome-coronavirus (SARS-CoV) and the new coronavirus (SARS-CoV-2) that is causing the serious coronavirus disease 2019 (COVID-19) epidemic. Here, we present cryo-electron microscopy structures of full-length human ACE2 in the presence of the 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 angstroms, with a local resolution of 3.5 angstroms 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 of ACE2 mediating homodimerization. The RBD is recognized by the extracellular peptidase domain of ACE2 mainly through polar residues. These findings provide important insights into the molecular basis for coronavirus recognition and infection.</AbstractText><CopyrightInformation>Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yan</LastName><ForeName>Renhong</ForeName><Initials>R</Initials><Identifier Source="ORCID">0000-0002-7122-6547</Identifier><AffiliationInfo><Affiliation>Key Laboratory of Structural Biology of Zhejiang Province, Institute of Biology, Westlake Institute for Advanced Study, 18 Shilongshan Road, Hangzhou 310024, Zhejiang Province, China.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>School of Life Sciences, Westlake University, 18 Shilongshan Road, Hangzhou 310024, Zhejiang Province, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y" EqualContrib="Y"><LastName>Zhang</LastName><ForeName>Yuanyuan</ForeName><Initials>Y</Initials><Identifier Source="ORCID">0000-0002-2500-0010</Identifier><AffiliationInfo><Affiliation>Key Laboratory of Structural Biology of Zhejiang Province, Institute of Biology, Westlake Institute for Advanced Study, 18 Shilongshan Road, Hangzhou 310024, Zhejiang Province, China.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>School of Life Sciences, Westlake University, 18 Shilongshan Road, Hangzhou 310024, Zhejiang Province, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y" EqualContrib="Y"><LastName>Li</LastName><ForeName>Yaning</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Xia</LastName><ForeName>Lu</ForeName><Initials>L</Initials><Identifier Source="ORCID">0000-0003-3007-3086</Identifier><AffiliationInfo><Affiliation>Key Laboratory of Structural Biology of Zhejiang Province, Institute of Biology, Westlake Institute for Advanced Study, 18 Shilongshan Road, Hangzhou 310024, Zhejiang Province, China.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>School of Life Sciences, Westlake University, 18 Shilongshan Road, Hangzhou 310024, Zhejiang Province, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Guo</LastName><ForeName>Yingying</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Key Laboratory of Structural Biology of Zhejiang Province, Institute of Biology, Westlake Institute for Advanced Study, 18 Shilongshan Road, Hangzhou 310024, Zhejiang Province, China.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>School of Life Sciences, Westlake University, 18 Shilongshan Road, Hangzhou 310024, Zhejiang Province, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhou</LastName><ForeName>Qiang</ForeName><Initials>Q</Initials><Identifier Source="ORCID">0000-0002-6237-8813</Identifier><AffiliationInfo><Affiliation>Key Laboratory of Structural Biology of Zhejiang Province, Institute of Biology, Westlake Institute for Advanced Study, 18 Shilongshan Road, Hangzhou 310024, Zhejiang Province, China. zhouqiang@westlake.edu.cn.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>School of Life Sciences, Westlake University, 18 Shilongshan Road, Hangzhou 310024, Zhejiang Province, China.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D059040">Video-Audio Media</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>03</Month><Day>04</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Science</MedlineTA><NlmUniqueID>0404511</NlmUniqueID><ISSNLinking>0036-8075</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance 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MajorTopicYN="N">SARS Virus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName><QualifierName UI="Q000648" MajorTopicYN="Y">ultrastructure</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>02</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>03</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>3</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>4</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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