Afsaneh Najafi Sarpiri - Department of Biology, Science School, Yazd University, Yazd, Iran

Backgrounds: Duchenne muscular dystrophy is a progressive neuromuscular disease that leadsto difficulties in movement and premature death. This disease is a X-linked recessive disorder.DMD disease is caused by mutations in DMD gene (encoding dystrophin) that destroy theproduction of dystrophin in muscle. Muscles without dystrophin are sensitive to damage, thatcause progressive loss of muscle tissue and function. In this study, a single nucleotidepolymorphism (SNP) in NCBI was selected in the DMD gene for investigation.Materials and Methods: In (rs۱۲۸۶۲۶۲۳۶ G>T), the effect of conversion of alanine, ahydrophobic amino acid to aspartic acid, a hydrophilic amino acid on protein structure wasassessed using SIFT, PROVEAN and I-Mutant databases.Results: In this study, the SIFT database showed that Substitution at pos. ۱۶۸ from A to D ispredicted to AFFECT PROTEIN FUNCTION with a score of ۰.۰۱. The variant was thenexamined in the PROVEAN database. According to the PROVEAN database, the A۱۶۸D variantwith PROVEAN score = -۴.۵۱۳ (cutoff = -۲.۵) is predicted to be a DELETERIOUS variant.Finally, the variant was assessed using the I-MUTANT database [this database is Predictor ofProtein Stability Changes upon Mutations] and DDG = -۰.۵۲ was obtained (DDG less than ۰:Decrease Stability.Conclusion: These results suggest that the A۱۶۸D variant in the rs۱۲۸۶۲۶۲۳۶ region of theDMD gene probably is a Deleterious variant and affects protein function. However, moreinvestigation is needed to clarify this.

DMD Gene, Duchenne muscular dystrophy, SNP, Pathogenic variant