Identification and Structural Comparison Of Deleterious Mutations In Nssnps of Cyp1b1 Gene In Glaucoma

Research Article
Jincy Anna Jomy and Rao Sethumadhavan*
DOI: 
xxx-xxxx-xxxx
Subject: 
Science
KeyWords: 
Glaucoma, CYP1B1, AHR, protein docking, free energy.
Abstract: 

We assessed the Single Nucleotide Polymorphisms (SNPs) that can change the expression and function in CYP1B1 gene using computational approaches. To study the connections among hereditary changes andphenotypic variation, distinctive omputational methods like Sorting Intolerant from Tolerant (SIFT),Polymorphism Phenotyping (PolyPhen) and I-Mutant 3.0 are examined. There were 54 missensemuatation; in this we watched 36 variations that were ruinous. We got 41 non-synonymous SNPs (nsSNPs) (72.92%) to be deleterious by SIFT. I- Mutant 3.0 were screening 52 (96.29%) deleteriousmutants and 40 nsSNPs (74.07%) as from Polyphen-2. Cation-π interactions in protein structures arerecognized and investigated the Arg, Lys interractions with π (Phe, Tyr or Trp) residues and their part instructural stability. Accordingly, modeling of these variations was implemented to comprehend theadjustment in their compliance concerning the native CYP1B1 by processing their root mean squaredeviation (RMSD). Those missense changes were because of loss of stability in their mutant structures ofCYP1B1. The native and mutants were docked with the substrate 4f31 to clarify the substrate bindingefficiencies of those hindering missense transformations. This was affirmed by figuring their total energiesby utilizing GROMOS 96 force field and these changes were cross approved with computational projects.Here we presume that our work could recover the genes related missense mutations precisely as we crossvalidated some of our outcomes with tentatively demonstrated results by other research groups.