| Autor: |
Atwah, Banan, Alghamdi, Saad, Saeedi, Nizar H., Alzahrani, Abdulrahman, Alghamdi, Rashed Mohammed, Akber, Asif Hussain, Al Qahtani, Mohammed Yahya, Yahya Mujarribi, Atiah Abkar, Al Qahtani, Saeed Saleh, Faqihi, Ahmed Mohammed, Kamal, Mohammad Azhar |
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| Zdroj: |
Advancements in Life Sciences; May2024, Vol. 11 Issue 2, p430-437, 8p |
| Abstrakt: |
Background: ZIKV is one of the re-emerging arboviruses (viruses carried by arthropods), which is spread through the Aedes mosquito. It is an RNA virus with only one strand that is appropriate to the family Flaviviridae's Flavivirus (genus) & has been linked to other Flaviviruses such as the West Nile virus, chikungunya virus, & dengue (DENV) virus. The envelope, precursor membrane, and capsid are three structural proteins, and seven nonstructural proteins are also encoded by the Zika virus genome. Methods: We conducted an in-silico analysis of the Zika virus' MTase domain protein for this publication. We predicted that methylation would play a significant role in the available Prosite, Pfam, and InterProScan tools to aid in locating the MTase domain. Along with alignment, amino acid composition, charged amino acids, atomic level studies, & molecular weight, we also make predictions for these variables, including theoretical Pi. Results: We also examine the MTase domain's simulated structure (alpha helix, beta sheet, turn) and its specifics, including secondary structure. We also pinpoint the locations where proteins, DNA, and RNA bind. Potential phosphorylation sites can be found on the Ser, Thr, and Tyr residues in the MTase domain. Conclusion: These outcomes imply a complicated interaction between different phosphorylation modifications that modulates the activity of the MTase domain. To fully appreciate the auxiliary and practical perspectives and to clarify the varied roles of PTM in the MTase domain will be a primary goal of future study. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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