Studying the Effects of ACE2 Mutations on the Stability, Dynamics, and Dissociation Process of SARS-CoV-2 S1/hACE2 Complexes.
J Proteome Res
; 19(11): 4609-4623, 2020 11 06.
Article
in English
| MEDLINE | ID: covidwho-960272
ABSTRACT
A highly infectious coronavirus, SARS-CoV-2, has spread in many countries. This virus recognizes its receptor, angiotensin-converting enzyme 2 (ACE2), using the receptor binding domain of its spike protein subunit S1. Many missense mutations are reported in various human populations for the ACE2 gene. In the current study, we predict the affinity of many ACE2 variants for binding to S1 protein using different computational approaches. The dissociation process of S1 from some variants of ACE2 is studied in the current work by molecular dynamics approaches. We study the relation between structural dynamics of ACE2 in closed and open states and its affinity for S1 protein of SARS-CoV-2.
Keywords
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Peptidyl-Dipeptidase A
/
Mutation, Missense
/
Spike Glycoprotein, Coronavirus
Type of study:
Experimental Studies
/
Prognostic study
Topics:
Variants
Limits:
Humans
Country/Region as subject:
Asia
Language:
English
Journal:
J Proteome Res
Journal subject:
Biochemistry
Year:
2020
Document Type:
Article
Affiliation country:
Acs.jproteome.0c00348
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