cancer-research-structural-biochemistry-2019-posters

Page 48

Volume 3

August 5-6, 2019 | Singapore

CANCER RESEARCH AND PHARMACOLOGY

STRUCTURAL BIOCHEMISTRY, STEM CELLS AND MOLECULAR BIOLOGY

International Conference on

International Congress on

Cancer Research 2019 & Structural Biochemistry 2019

August 5-6, 2019

Journal of Cancer and Metastasis Research

Computational analysis of single nucleotide polymorphisms (SNPs) in human ATP1-A2

gene

Afra M Bkrye

University of Bahri, Sudan

BACKGROUND

: In this study we analyzed the effect of genetic mutations mainly Single nucleotide polymorphisms (SNPs)

mutations that can alter the expression and functions of ATP1A2 gene as gene had been candidate to cause Migraine.

METHODS

:ATP1A2 gene was investigated in dbSNP/NCBI database in June 2016 and we used different computational analysis

approach. Deleterious nsSNPs were predicted by SIFT and Polyphen-2 softwares. Then the damaging nsSNPs were submitted

to I- mutant to Predict the change in stability due to mutation and PHD-SNP and SNPS&GO software used to demonstrate the

relationship between SNP and related Migraine Protein structural analysis of amino acid variants was performed by Project

Hope. To highlight genetic interactions of ATP1A2 we used Gene MANIA software.

RESULTS

: Gena mania revealed that ATP1A2Gene encodes for the α2 subunit of ATPase Na+/ K. The SNPs sequence of

ATP1A2 gene was collected from NCBI; 2576of them [Homo sapiens] only From sift and polyphen-2 software the high score

deleterious SNPs were found as following: (rs28933401), (rs368405677), (rs121918612), (rs121918614), (rs121918615),

(rs121918618), (rs121918619), ( rs200425518), (rs181618883) and (rs149144720) Which analysis in Project HOPE software

to analyzed the changing in amino acid properties and domains, which found among these (rs). (rs28933401), (rs368405677),

(rs121918612) have 100% mutation. Additionally, I-Mutant and PHD-SNPs and SNP&GO showed decrease instability for these

nsSNP sup on mutation. Protein structural analysis with these amino acid variants was performed by using I-Mutant, Swiss PDB

viewer, to check their molecular dynamics and energy minimization calculations.

CONCLUSION

: in this study we found R689Q, T378N, G301R, D718N, P979L, T415M, R171W, A688P, A297T and G855E

mutations in ATP1A2 gene could directly or indirectly destabilize the amino acid interactions and hydrogen bonds networks thus

explaining the functional deviations of protein To some extent mutations in ATP1A2 gene could directly or indirectly destabilize

the amino acid interactions and hydrogen bonds networks thus explaining the functional deviations of protein to some extent.

Biography

Afra M Bkrye has completed MSC in Biotechnology at Sudan academy of science and technology. Currently she is working as lecturer

at Bahri University, department of biochemistry and molecular biology.