Open AccessVariety of Spike Protein in COVID-19 Mutation: Stability, Effectiveness and Outbreak Rate as a Target for Vaccine and Therapeutic Development
Author(s) -
Majid Monajjemi,
Ф. Моллаамин,
A. S. Shekarabi,
Amin Ghadami
Publication year - 2020
Publication title -
biointerface research in applied chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.216
H-Index - 11
ISSN - 2069-5837
DOI - 10.33263/briac113.1001610026
Subject(s) - computational biology , coronavirus , genome , homology modeling , biology , polyadenylation , protein structure , antiparallel (mathematics) , virology , genetics , covid-19 , rna , gene , physics , medicine , biochemistry , disease , pathology , quantum mechanics , magnetic field , infectious disease (medical specialty) , enzyme
The structure of β-coronavirus MERS-CoV S1-CTD demonstrated an interesting subject of how two structurally similar viral RBDs recognize different protein receptors. Same as SARS-CoV, the S1-CTD, MERS-CoV S1-CTD viruses also contains two subdomains, but, in contrast to the loop-dominated MERS-CoV, RBM contains a 4-stranded antiparallel β-sheet, showing a relatively flat surface to bind DPP4. The protein sequences were obtained from NCBI web sites, and the proteins of COVID-19, such as protein sequences, were applied for analyzing the conserved domain. Some proteins were also utilized for constructing 3-D structures via homology modeling. We also show that N-terminal deletions of alpha 2 that no longer block STAT1 nuclear import. Covid-19 spike protein structures, along with peptide-like inhibitor structure of the SARS-CoV-2 spike glycoprotein, including small-molecule inhibitors, have been simulated via Molecular dynamic and docking methods. Several genomes of various coronaviruses using BAST and MAFFT software have been evaluated, and a few genomes have been selected.