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Finding Pathogenic nsSNP’s and their structural effect on COPS2 using Molecular Dynamic Approach

View ORCID ProfileAshish Malik, Kajal Pande, Abhishek Kumar, Alekhya Vemula, R Madhuri, Vivek Chandramohan
doi: https://doi.org/10.1101/2020.10.12.333252
Ashish Malik
1BiSEP, Bioinformatics and Big data analytics, Department of Biotechnology, Siddaganga Institute of Technology, Tumkur
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  • ORCID record for Ashish Malik
Kajal Pande
1BiSEP, Bioinformatics and Big data analytics, Department of Biotechnology, Siddaganga Institute of Technology, Tumkur
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Abhishek Kumar
1BiSEP, Bioinformatics and Big data analytics, Department of Biotechnology, Siddaganga Institute of Technology, Tumkur
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Alekhya Vemula
1BiSEP, Bioinformatics and Big data analytics, Department of Biotechnology, Siddaganga Institute of Technology, Tumkur
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R Madhuri
1BiSEP, Bioinformatics and Big data analytics, Department of Biotechnology, Siddaganga Institute of Technology, Tumkur
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Vivek Chandramohan
2Department of Biotechnology, Siddaganga Institute of Technology, Tumkur
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  • For correspondence: vivek@sit.ac.in
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Abstract

COP9 Signalosome Subunit 2 is a highly conserved multiprotein complex which is involved in the cellular process and developmental process. It is one of the essential components in the COP9 Signalosome Complex (CSN). It is also involved in neuronal differentiation interacting with NIF3L1. The gene involved in neuronal differentiation is negatively regulated due to the transcription co-repressor interaction of NIF3L1 with COPS2. In the present study, we have evaluated the outcome for 90 non-synonymous single nucleotide polymorphisms (nsSNP’s) in COPS2 gene through computational tools. After the analysis, 4 SNP’s (S120C, N144S, Y159H, R173C) were found to be deleterious. The native and mutated structures were prepared using discovery studio and docked to check the interactions with NIF3L1.On the basis of ZDOCK score the top 3 mutations (N144S, Y159H, R173C) were screened out. Further to analyze the effect of amino acid substitution on the molecular structure of protein Molecular Dynamics simulation was carried out. Analysis based on RMSD, RMSF, RG, H-bond showed a significant deviation in the graph, which demonstrated conformation change and instability compared to the wild structure. As it is known mutations in COPS2 gene can disrupt the normal activity of the CSN2 protein which may cause neuronal differentiation. Our results showed N144S, Y159H and R173C mutations are to be more pathogenic and may cause disease

Competing Interest Statement

The authors have declared no competing interest.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
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Posted October 12, 2020.
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Finding Pathogenic nsSNP’s and their structural effect on COPS2 using Molecular Dynamic Approach
Ashish Malik, Kajal Pande, Abhishek Kumar, Alekhya Vemula, R Madhuri, Vivek Chandramohan
bioRxiv 2020.10.12.333252; doi: https://doi.org/10.1101/2020.10.12.333252
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Finding Pathogenic nsSNP’s and their structural effect on COPS2 using Molecular Dynamic Approach
Ashish Malik, Kajal Pande, Abhishek Kumar, Alekhya Vemula, R Madhuri, Vivek Chandramohan
bioRxiv 2020.10.12.333252; doi: https://doi.org/10.1101/2020.10.12.333252

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