tetano
Editor, Senior Moderator
J Proteome Res
. 2020 Jul 27.
doi: 10.1021/acs.jproteome.0c00348. Online ahead of print.
Studying the Effects of ACE2 Mutations on Stability, Dynamics and Dissociation Process of SARS-CoV-2 S1/hACE2 Complexes
Hamid Hadi-Alijanvand, Maryam Rouhani
Abstract
A highly infectious coronavirus, SARS-CoV-2, spreads in many countries. This virus recognizes its receptor, angiotensin-converting enzyme 2 (ACE2) using receptor binding domain of its spike protein subunit S1. Many missense mutations are reported in various human populations for ACE2 gene. In 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 current work by molecular dynamic approaches. We study the relation between structural dynamics of ACE2 in close/open states and its affinity for S1 protein of SARS-CoV-2.
. 2020 Jul 27.
doi: 10.1021/acs.jproteome.0c00348. Online ahead of print.
Studying the Effects of ACE2 Mutations on Stability, Dynamics and Dissociation Process of SARS-CoV-2 S1/hACE2 Complexes
Hamid Hadi-Alijanvand, Maryam Rouhani
- PMID: 32786692
- DOI: 10.1021/acs.jproteome.0c00348
Abstract
A highly infectious coronavirus, SARS-CoV-2, spreads in many countries. This virus recognizes its receptor, angiotensin-converting enzyme 2 (ACE2) using receptor binding domain of its spike protein subunit S1. Many missense mutations are reported in various human populations for ACE2 gene. In 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 current work by molecular dynamic approaches. We study the relation between structural dynamics of ACE2 in close/open states and its affinity for S1 protein of SARS-CoV-2.