Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2
Identifieur interne : 000063 ( Pmc/Checkpoint ); précédent : 000062; suivant : 000064Structural basis for the recognition of 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.) [ 0036-8075 ] ; 2020.
Abstract
Scientists are racing to learn the secrets of severe acute respiratory
syndrome–coronavirus 2 (SARS-CoV-2), which is the cause of the pandemic disease
COVID-19. The first step in viral entry is the binding of the viral trimeric spike protein
to the human receptor angiotensin-converting enzyme 2 (ACE2). Yan
Url:
DOI: 10.1126/science.abb2762
PubMed: 32132184
PubMed Central: 7164635
Affiliations:
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PMC:7164635Le document en format XML
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<author><name sortKey="Zhou, Qiang" sort="Zhou, Qiang" uniqKey="Zhou Q" first="Qiang" last="Zhou">Qiang Zhou</name>
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<front><div type="abstract" xml:lang="en"><title>How SARS-CoV-2 binds to human cells</title>
<p>Scientists are racing to learn the secrets of severe acute respiratory
syndrome–coronavirus 2 (SARS-CoV-2), which is the cause of the pandemic disease
COVID-19. The first step in viral entry is the binding of the viral trimeric spike protein
to the human receptor angiotensin-converting enzyme 2 (ACE2). Yan <italic>et al.</italic>
present the structure of human ACE2 in complex with a membrane protein that it chaperones,
B<sup>0</sup>
AT1. In the context of this complex, ACE2 is a dimer. A further structure
shows how the receptor binding domain of SARS-CoV-2 interacts with ACE2 and suggests that
it is possible that two trimeric spike proteins bind to an ACE2 dimer. The structures
provide a basis for the development of therapeutics targeting this crucial
interaction.</p>
<p><italic>Science</italic>
, this issue p. <ext-link ext-link-type="doi" xlink:href="10.1126/science.abb2762">1444</ext-link>
</p>
</div>
</front>
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</TEI>
<pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Science</journal-id>
<journal-id journal-id-type="iso-abbrev">Science</journal-id>
<journal-id journal-id-type="publisher-id">SCIENCE</journal-id>
<journal-id journal-id-type="hwp">science</journal-id>
<journal-title-group><journal-title>Science (New York, N.y.)</journal-title>
</journal-title-group>
<issn pub-type="ppub">0036-8075</issn>
<issn pub-type="epub">1095-9203</issn>
<publisher><publisher-name>American Association for the Advancement of Science</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">32132184</article-id>
<article-id pub-id-type="pmc">7164635</article-id>
<article-id pub-id-type="publisher-id">abb2762</article-id>
<article-id pub-id-type="doi">10.1126/science.abb2762</article-id>
<article-categories><subj-group subj-group-type="article-type"><subject>Research Article</subject>
</subj-group>
<subj-group subj-group-type="heading"><subject>Research Articles</subject>
</subj-group>
<subj-group subj-group-type="legacy-article-type"><subject>R-Articles</subject>
</subj-group>
<subj-group subj-group-type="field"><subject>Biochem</subject>
<subject>Cell Biol</subject>
</subj-group>
</article-categories>
<title-group><article-title>Structural basis for the recognition of SARS-CoV-2 by full-length human
ACE2</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><contrib-id contrib-id-type="orcid" authenticated="true">https://orcid.org/0000-0002-7122-6547</contrib-id>
<name><surname>Yan</surname>
<given-names>Renhong</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>1</sup>
</xref>
<xref ref-type="aff" rid="aff2"><sup>2</sup>
</xref>
</contrib>
<contrib contrib-type="author"><contrib-id contrib-id-type="orcid" authenticated="true">https://orcid.org/0000-0002-2500-0010</contrib-id>
<name><surname>Zhang</surname>
<given-names>Yuanyuan</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>1</sup>
</xref>
<xref ref-type="aff" rid="aff2"><sup>2</sup>
</xref>
<xref ref-type="author-notes" rid="afn1">*</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Li</surname>
<given-names>Yaning</given-names>
</name>
<xref ref-type="aff" rid="aff3"><sup>3</sup>
</xref>
<xref ref-type="author-notes" rid="afn1">*</xref>
</contrib>
<contrib contrib-type="author"><contrib-id contrib-id-type="orcid" authenticated="true">https://orcid.org/0000-0003-3007-3086</contrib-id>
<name><surname>Xia</surname>
<given-names>Lu</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>1</sup>
</xref>
<xref ref-type="aff" rid="aff2"><sup>2</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Guo</surname>
<given-names>Yingying</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>1</sup>
</xref>
<xref ref-type="aff" rid="aff2"><sup>2</sup>
</xref>
</contrib>
<contrib contrib-type="author"><contrib-id contrib-id-type="orcid" authenticated="true">https://orcid.org/0000-0002-6237-8813</contrib-id>
<name><surname>Zhou</surname>
<given-names>Qiang</given-names>
</name>
<xref ref-type="award" rid="award586138"></xref>
<xref ref-type="award" rid="award594232"></xref>
<xref ref-type="aff" rid="aff1"><sup>1</sup>
</xref>
<xref ref-type="aff" rid="aff2"><sup>2</sup>
</xref>
<xref ref-type="corresp" rid="cor1">†</xref>
</contrib>
<aff id="aff1"><label>1</label>
Key Laboratory of Structural Biology of Zhejiang Province, Institute of Biology, Westlake Institute for Advanced Study, 18 Shilongshan Road, Hangzhou 310024, Zhejiang Province, China.</aff>
<aff id="aff2"><label>2</label>
School of Life Sciences, Westlake University, 18 Shilongshan Road, Hangzhou 310024, Zhejiang Province, China.</aff>
<aff id="aff3"><label>3</label>
Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.</aff>
</contrib-group>
<author-notes><fn id="afn1" fn-type="equal"><label>*</label>
<p>These authors contributed equally to this work.</p>
</fn>
<corresp id="cor1"><label>†</label>
Corresponding author. Email: <email xlink:href="zhouqiang@westlake.edu.cn">zhouqiang@westlake.edu.cn</email>
</corresp>
</author-notes>
<pub-date pub-type="ppub"><day>27</day>
<month>3</month>
<year>2020</year>
</pub-date>
<pub-date pub-type="epub"><day>04</day>
<month>3</month>
<year>2020</year>
</pub-date>
<volume>367</volume>
<issue>6485</issue>
<fpage>1444</fpage>
<lpage>1448</lpage>
<history><date date-type="received"><day>12</day>
<month>2</month>
<year>2020</year>
</date>
<date date-type="accepted"><day>03</day>
<month>3</month>
<year>2020</year>
</date>
</history>
<permissions><copyright-statement>Copyright © 2020 The Authors, some rights reserved; exclusive
licensee American Association for the Advancement of Science. No claim to original U.S.
Government Works</copyright-statement>
<copyright-year>2020</copyright-year>
<copyright-holder>AAAS</copyright-holder>
<license license-type="open-access" xlink:href="http://creativecommons.org/licenses/by/4.0/"><ali:license_ref specific-use="vor" start_date="2020-03-04">https://creativecommons.org/licenses/by/4.0/</ali:license_ref>
<license-p>This open access article is distributed under <ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by/4.0/">Creative Commons Attribution License 4.0 (CC BY)</ext-link>
.</license-p>
</license>
</permissions>
<abstract abstract-type="editor"><title>How SARS-CoV-2 binds to human cells</title>
<p>Scientists are racing to learn the secrets of severe acute respiratory
syndrome–coronavirus 2 (SARS-CoV-2), which is the cause of the pandemic disease
COVID-19. The first step in viral entry is the binding of the viral trimeric spike protein
to the human receptor angiotensin-converting enzyme 2 (ACE2). Yan <italic>et al.</italic>
present the structure of human ACE2 in complex with a membrane protein that it chaperones,
B<sup>0</sup>
AT1. In the context of this complex, ACE2 is a dimer. A further structure
shows how the receptor binding domain of SARS-CoV-2 interacts with ACE2 and suggests that
it is possible that two trimeric spike proteins bind to an ACE2 dimer. The structures
provide a basis for the development of therapeutics targeting this crucial
interaction.</p>
<p><italic>Science</italic>
, this issue p. <ext-link ext-link-type="doi" xlink:href="10.1126/science.abb2762">1444</ext-link>
</p>
</abstract>
<abstract abstract-type="teaser"><p>Insight into how SARS-CoV-2 binds its human receptor could provide a basis for the
development of therapeutics.</p>
</abstract>
<abstract><p>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.</p>
</abstract>
<funding-group><award-group id="award586138"><funding-source><institution-wrap><institution-id institution-id-type="doi">http://dx.doi.org/10.13039/501100001809</institution-id>
<institution>National Natural Science Foundation of China</institution>
</institution-wrap>
</funding-source>
<award-id>31971123</award-id>
</award-group>
<award-group id="award586141"><funding-source><institution-wrap><institution-id institution-id-type="doi">http://dx.doi.org/10.13039/501100001809</institution-id>
<institution>National Natural Science Foundation of China</institution>
</institution-wrap>
</funding-source>
<award-id>81920108015</award-id>
</award-group>
<award-group id="award586171"><funding-source><institution-wrap><institution-id institution-id-type="doi">http://dx.doi.org/10.13039/501100001809</institution-id>
<institution>National Natural Science Foundation of China</institution>
</institution-wrap>
</funding-source>
<award-id>31930059</award-id>
</award-group>
<award-group id="award586172"><funding-source><institution-wrap><institution>Key R&D Program of Zhejiang Province</institution>
</institution-wrap>
</funding-source>
<award-id>2020C04001</award-id>
</award-group>
<award-group id="award594232"><funding-source><institution-wrap><institution>the SARS-CoV-2 emergency project of the Science and Technology Department
of Zhejiang Province</institution>
</institution-wrap>
</funding-source>
<award-id>2020C03129</award-id>
</award-group>
</funding-group>
<custom-meta-group><custom-meta><meta-name>Number-color-figs</meta-name>
<meta-value>5</meta-value>
</custom-meta>
<custom-meta><meta-name>Number-figs</meta-name>
<meta-value>5</meta-value>
</custom-meta>
<custom-meta><meta-name>Editor</meta-name>
<meta-value>Valda Vinson</meta-value>
</custom-meta>
<custom-meta><meta-name>Copyeditor</meta-name>
<meta-value>Amelia Beyna</meta-value>
</custom-meta>
</custom-meta-group>
</article-meta>
</front>
</pmc>
<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="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="Xia, Lu" sort="Xia, Lu" uniqKey="Xia L" first="Lu" last="Xia">Lu Xia</name>
<name sortKey="Yan, Renhong" sort="Yan, Renhong" uniqKey="Yan R" first="Renhong" last="Yan">Renhong Yan</name>
<name sortKey="Zhang, Yuanyuan" sort="Zhang, Yuanyuan" uniqKey="Zhang Y" first="Yuanyuan" last="Zhang">Yuanyuan Zhang</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>
<name sortKey="Zhou, Qiang" sort="Zhou, Qiang" uniqKey="Zhou Q" first="Qiang" last="Zhou">Qiang Zhou</name>
</country>
</tree>
</affiliations>
</record>
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