The Sequence provides insight into a structure-based investigation of the critical Japanese encephalitis domain | [Bioscience Research • 2023]

Author(s):

1. Ziaullah M Sain: Department of Microbiology, Faculty of Medicine, Rabigh, King Abdulaziz University, Jeddah. 21589., Saudi Arabia

2. Asif Hussain Akber: Central Military Laboratory and Blood Bank Department - Virology Division, Prince Sultan Military Medical City, Riyadh 12233, Saudi Arabia

3. Yousef Mutad Al Harbi: Central Military Laboratory and Blood Bank Department - Virology Division, Prince Sultan Military Medical City, Riyadh 12233, Saudi Arabia

4. Khaled Ahmed Alahmari: Central Military Laboratory and Blood Bank Department - ED Lab Division, Prince Sultan Military Medical City, Riyadh 12233, Saudi Arabia

5. Lahiq Ahmad Aseri: Central Military Laboratory and Blood Bank Department - Hematology Lab Division, Prince Sultan Military Medical City, Riyadh 12233, Saudi Arabia

6. Awadh Ali Ayed Alqarni: Central Military Laboratory and Blood Bank Department - ED Lab Division, Prince Sultan Military Medical City, Riyadh 12233, Saudi Arabia

7. Osama Faqihi: Respiratory Therapy Department, King Fahad Military Medical Complex Dhahran, Saudi Arabia

8. Nabeela Al-Abdullah: King Abdulaziz University, Faculty of Nursing, Public Health Department, Infection Control Unit, King Abdulaziz University Hospital Jeddah, Saudi Arabia

9. Qamre Alam: Molecular Genomics and Precision Medicine Department, ExpressMed Diagnostic and Research, Block, 359, Zinj, Kingdom of Bahrain

Abstract:

Mosquitoes transmit the flavivirus known as the Japanese encephalitis virus (JEV), which is related to dengue, yellow fever, and other viruses. In this manuscript, we have done an insilico examination of the JEV (Japanese encephalitis) protein (Helicase ATP binding domain). We predicted a crucial part that belongs to the DEAH-Box RNA helicase. The available tools Prosite, Pfam, and Inter ProScan help to identify the helicase ATP binding domain (HABD). We also predict alignment, amino acid composition, charged amino acid, atomic level study, and molecular weight, including theoretical Pi. We also study the modelled structure of the helicase ATP binding domain (helices, beta turns) and their details, including secondary structure. This family takes into account an enormous number of RNA helicases. The Ramachandran plot was used for structure validation, including the topology observation of the helicase domain protein. The domain contains strands, a-helix, and circles. The part has a beta-turn, and their deposits are separate between the under 7å. The numeral of collections per turn for alpha helices, the helix contributes to the extent of the deviancy of the helix geometry as of an ideal helix. We also investigate the protein, DNA, and RNA binding sites. In the current research, we appraise the structure-based information and its composition (amino acid and atomic), helices, beta turns, and binding sites' details.

Page(s): 667-676

DOI: DOI not available

Published: Journal: Bioscience Research, Volume: 20, Issue: 3, Year: 2023

Keywords:

ahelix , Prosite , binding sites , Pfam , Ramachandran plot , Secondary structure , InterProScan

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