| Makale Türü |
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| Dergi Adı | Biointerface Research in Applied Chemistry | ||
| Dergi ISSN | 2069-5837 Wos Dergi Scopus Dergi | ||
| Makale Dili | İngilizce | Basım Tarihi | 06-2021 |
| Cilt / Sayı / Sayfa | 11 / 3 / 10016–10026 | DOI | 10.33263/BRIAC113.1001610026 |
| 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 |
| Atıf Sayıları | |
| Web of Science | 4 |
| Scopus | 3 |
| Dergi Adı | Biointerface Research in Applied Chemistry |
| Yayıncı | AMG Transcend Association |
| Açık Erişim | Hayır |
| ISSN | 2069-5837 |
| E-ISSN | 2069-5837 |
| CiteScore | 6,4 |
| SJR | 0,381 |
| SNIP | 0,553 |