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Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2

Identifieur interne : 000204 ( Main/Exploration ); précédent : 000203; suivant : 000205

Structural 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 :

RBID : PMC:7164635

Descripteurs français

English descriptors

Abstract

How SARS-CoV-2 binds to human cells

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 et al.present the structure of human ACE2 in complex with a membrane protein that it chaperones, B0AT1. 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.

Science, this issue p. 1444


Url:
DOI: 10.1126/science.abb2762
PubMed: 32132184
PubMed Central: 7164635


Affiliations:


Links toward previous steps (curation, corpus...)


Le document en format XML

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<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>
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</record>

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   |étape=   Exploration
   |type=    RBID
   |clé=     PMC:7164635
   |texte=   Structural basis for the recognition of SARS-CoV-2 by full-length human
ACE2
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i   -Sk "pubmed:32132184" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
       | NlmPubMed2Wicri -a SrasV1 

Wicri

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