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About:
Structural basis for the recognition of the 2019-nCoV by human ACE2
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covidontheweb.inria.fr
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Academic Article
research paper
schema:ScholarlyArticle
isDefinedBy
Covid-on-the-Web dataset
title
Structural basis for the recognition of the 2019-nCoV by human ACE2
Creator
Guo, Yingying
Xia, Lu
Zhang, Yuanyuan
Zhou, Qiang
Yan, Renhong
source
BioRxiv; MedRxiv
abstract
Angiotensin-converting enzyme 2 (ACE2) has been suggested to be the cellular receptor for the new coronavirus (2019-nCoV) that is causing the coronavirus disease 2019 (COVID-19). Like other coronaviruses such as the SARS-CoV, the 2019-nCoV uses the receptor binding domain (RBD) of the surface spike glycoprotein (S protein) to engage ACE2. We most recently determined the structure of the full-length human ACE2 in complex with a neutral amino acid transporter B0AT1. Here we report the cryo-EM structure of the full-length human ACE2 bound to the RBD of the 2019-nCoV at an overall resolution of 2.9 Å in the presence of B0AT1. The local resolution at the ACE2-RBD interface is 3.5 Å, allowing analysis of the detailed interactions between the RBD and the receptor. Similar to that for the SARS-CoV, the RBD of the 2019-nCoV is recognized by the extracellular peptidase domain (PD) of ACE2 mainly through polar residues. Pairwise comparison reveals a number of variations that may determine the different affinities between ACE2 and the RBDs from these two related viruses.
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2020-02-20
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bibo:doi
10.1101/2020.02.19.956946
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biorxiv
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563ba81d1b21b4937166a4f5976767ce7be69f9f
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https://doi.org/10.1101/2020.02.19.956946
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Structural basis for the recognition of the 2019-nCoV by human ACE2
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bioRxiv
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covid:563ba81d1b21b4937166a4f5976767ce7be69f9f#body_text
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named entity 'engage'
named entity 'acid'
named entity 'structure'
named entity 'binding domain'
named entity 'RESOLUTION'
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