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3D Structure modeling & analysis of transmembrane protein EVI2A from Homo sapiens
1 , 2 , 3 , 4 , 5, 6 , * 1
1  School of Biotechnology and Bioinformatics, D Y Patil Deemed to be University, Navi Mumbai, Maharashtra, India
2  Amity Institute of Biotechnology, Amity University Mumbai, Maharashtra, India
3  Department of Pharmaceutical Chemistry, Bhujbal Knowledge City, MET's Institute of Pharmacy, Adgaon, Nashik, Maharashtra, India
4  Proteomics Center, Institute of Biochemistry, Vilnius University Life Sciences Center, Vilnius, Lithuania
5  MAP Kinase Resource, Bioinformatics, Melchiorstrasse 9, Bern 3027, Switzerland
6  Department of Microbiology, Immunology and Genetics, Max F. Perutz Laboratories, University of Vienna, 1030 Vienna, Austria

Published: 31 October 2018 by MDPI in 4th International Electronic Conference on Medicinal Chemistry session ECMC-4
Abstract:

Protein EVI2A (Ecotropic viral integration site 2A) is a type 1 single pass membrane protein containing 236 amino acid residues. EVI2A is associated with several human diseases such as schizophrenia and numerous malignancies including breast and ovarian cancers.

Protein 3D structure helps in understanding the molecular function of the proteins and their important role in the biological scenario if any. Till date no 3D structure of protein EVI2A has been reported in public or private databases. To fill that gap, we evaluated some computational models including comparative methods, de novo approach, ab initio and threading based methods. The multiple models, including 3D model from I-Tasser, afforded a good agreement of output and structural features. A complete model of protein EVI2A was validated by ProSa and Ramachandran analyses. Molecular dynamics (MD) simulations were performed and analyzed using the GROMACS package and active site prediction was carried out using CASTp. The predicted model could be a starting point for structural biologists, drug discovery groups, and scientific community to further enhance their studies.

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Keywords: EVI2A, I-Tasser, Dyamic Simulation, Protein Modeling, De novo
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