Abstract
IN SILICO ANALYSIS, HOMOLOGY MODELLING AND MOLECULAR DOCKING OF SINGLE NUCLEOTIDE POLYMORPHISMS IN HUMAN HER2/ERBB2 GENE

Jemimah Joji George and Kinnari N. Mistry*

ABSTRACT

HER2/ErbB2 Gene is known to be a key player in the pathogenesis of several human cancers. The HER2 receptors were amplified and resulted in overexpression of HER2 protein, which has been associated with tumor cell proliferation and cancer progression. Our study's main objectives are to evaluate and find the various tolerated, deleterious, damaging nsSNPs, their disease-causing ability, and the effect of those mutations on the stability of protein structure to find the molecular phenotypic effects of these nsSNPs and perform homology modeling and docking of ErbB2 gene. In our study, different variants of the Erbb2 gene associated with the other diseases were obtained using dbSNP and Disgenet. Variants associated with the disease were processed through SIFT analysis, and the variants with the lowest score (0.00-0.05) were selected. They were further analyzed through SNP & GO, and the mutation with the highest score (> 0.5) was found to be a disease-associated mutation. I-Tasser platform was used to perform homology modeling and was further validated by the Ramachandran plot. Molecular Docking of Model (associated disease) against drugs was performed by Py-Rx. The above analyses found that the mutation with the lowest score (SIFT) and highest Score (SNP and Go) were associated with Breast Cancer and Glioma. Drugs that showed the highest binding affinity with the model protein provide a new insight for ErbB2 as a drug target. Thus, it is concluded that several damaging, deleterious nsSNPS are highly disease-causing, changing the stability of protein structure, and different synthetic and natural drugs showed a high binding affinity with the protein model. So these drugs can be used in determining an effective treatment in the future.

Keywords: Erbb2 Gene; Variants; Mutation; Disease; Cancer.


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