Title

Analysis of Hepatitis E virus (HEV) X-domain structural model

Authors

Vikram Thakur^1*, Pradeep Kumar²

Affiliation

¹Department of Virology, Postgraduate Institute of Medical Education and Research (PGIMER), Sec-12, Chandigarh, India;

²Faculty of Applied Sciences and Biotechnology, Shoolini University, Solan, (HP) India;

Email

vik5atif@gmail.com

Article Type

Hypothesis

Date

Received June 25, 2018; Revised June 26, 2018; Accepted June 30, 2018; Published July 31, 2018

Hepatitis E viral infection is now emerging as a global health concern, which needs to be addressed. Mechanism of viral replication and release is attributed by the different genomic component of HEV. However, few proteins/domain like X and Y domain remain unexplored, so we aim to explore the physiochemical, structural and functional features of HEV ORF-1 X domain. Molecular modeling of the unknown X domain was carried out using Phyre2 and Swiss Model. Active ligand binding sites were predicted using Phyre2. The X-domain protein found to be stable and acidic in nature with high thermostability and better hydrophilic property. Twelve binding sites were predicted along with putative transferase and catalytic functional activity. Homology modeling showed 10 binding sites along with Mg2+ and Zn2+ as metallic heterogen ligands binding to predicted ligand-binding sites. This study may help to decipher the role of this unexplored X-domain of HEV, thereby improving our understanding of the pathogenesis of HEV infection.

Keywords

Hepatitis E Virus, ORF1, X domain model, Ligand binding site.

Citation

Thakur & Kumar. Bioinformation 14(7): 398-403 (2018)

Edited by

P Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.