Hold your horses: The receptor-binding domains of SARS-CoV-2, SARS-CoV, and hCoV-NL63 bind equine ACE2.

Nawrath, Philipp; Wrobel, Antoni G

Nawrath, Philipp; Wrobel, Antoni G.

Nawrath P; Structural Biology of Disease Processes Laboratory, The Francis Crick Institute, London, UK.
Wrobel AG; Structural Biology of Disease Processes Laboratory, The Francis Crick Institute, London, UK. Electronic address: antoni.wrobel@crick.ac.uk.

Structure ; 30(10): 1367-1368, 2022 10 06.

Article in English | MEDLINE | ID: covidwho-2049939

ABSTRACT

ABSTRACT

In this issue of Structure, Lan and colleagues seek to identify regions on the ACE2 receptor and coronavirus spikes that are essential for the viral attachment. They achieve it through a detailed comparative analysis of the binding of coronaviruses NL63, SARS-CoV, and several SARS-CoV-2 variants with human and horse ACE2.

Subject(s)

COVID-19; Coronavirus NL63, Human; Angiotensin-Converting Enzyme 2; Animals; Horses; Humans; Peptidyl-Dipeptidase A/chemistry; Peptidyl-Dipeptidase A/metabolism; SARS-CoV-2

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Coronavirus NL63, Human / COVID-19 Topics: Variants Limits: Animals / Humans Language: English Journal: Structure Journal subject: Molecular Biology / Biochemistry / Biotechnology Year: 2022 Document Type: Article Affiliation country: J.str.2022.09.003

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