| Yazarlar (4) |
Majid Monajjemi
|
Dr. Öğr. Üyesi Fatemeh MOLLAAMIN
Kastamonu Üniversitesi |
|
Azadeh Sadat Shekarabi
|
|
Azam Ghadami
|
| Özet |
| 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 loopdominated 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 Nterminal 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. |
| Anahtar Kelimeler |
| COVID-19 | MERS-CoV RBM | Mutations | Spike protein |
| Makale Türü | Özgün Makale |
| Makale Alt Türü | SCOPUS dergilerinde yayımlanan tam makale |
| Dergi Adı | Biointerface Research in Applied Chemistry |
| Dergi ISSN | 2069-5837 |
| Dergi Tarandığı Indeksler | SCOPUS |
| Makale Dili | İngilizce |
| Basım Tarihi | 01-2021 |
| Cilt No | 11 |
| Sayı | 3 |
| Sayfalar | 10016 / 10026 |
| Doi Numarası | 10.33263/BRIAC113.1001610026 |
| Atıf Sayıları | |
| WoS | 4 |
| SCOPUS | 4 |
