Author(s): Sowmya Hari, S. Akilashree

Email(s): sowmya.se@velsuniv.ac.in

DOI: 10.5958/0974-360X.2019.00575.4   

Address: Sowmya Hari1*, S. Akilashree2
1,2Department of Bio-Engineering, School of Engineering, Vels Institute of Science, Technology and Advanced Studies (VISTAS), Pallavaram, Chennai-600117, Tamilnadu, India.
*Corresponding Author

Published In:   Volume - 12,      Issue - 7,     Year - 2019


ABSTRACT:
Alzheimer’s disease is a neurodegenerative disorder which is caused by several mutations in causative proteins like Amyloid Precursor Protein (APP), Presenilin1 (PSEN1), and Presenilin2 (PSEN2). Mutations in presenilin 2 lead to the overproduction of amyloid beta peptide which gets accumulated in the brain and causes neuron death. This result in Early Onset Alzheimer’s disease (EOAD) and there are around 17 mutations in presenilin 2 results in this disease condition. There are 3 isoforms of PSEN2 which are normally found in the cells. Three dimensional structure of presenilin 2 has not been determined; hence, in this study the structure of presenilin 2 was predicted using homology modeling. The 3dimensional structures are modeled using Modeller9.20, Swiss Model and Geno3D. The structures are validated using PROCHECK. The structure of Swiss Model was found to be more reliable with fewer amino acids in the disallowed region, followed by Modeller9.0 and Geno3D. These structures will be fundamental in determining the crystal structure of presenilin 2 and for drug discovery.


Cite this article:
Sowmya Hari, S. Akilashree. In Silico Homology Modeling of Presenilin 2- Therapeutic Target for Alzheimer’s disease. Research J. Pharm. and Tech. 2019; 12(7):3405-3409. doi: 10.5958/0974-360X.2019.00575.4

Cite(Electronic):
Sowmya Hari, S. Akilashree. In Silico Homology Modeling of Presenilin 2- Therapeutic Target for Alzheimer’s disease. Research J. Pharm. and Tech. 2019; 12(7):3405-3409. doi: 10.5958/0974-360X.2019.00575.4   Available on: https://rjptonline.org/AbstractView.aspx?PID=2019-12-7-50


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RNI: CHHENG00387/33/1/2008-TC                     
DOI: 10.5958/0974-360X 

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