Akademik Veri Yönetim Sistemi
3 th International Congress of Engineering and Natural Sciences, Ankara, Türkiye, 24 - 25 Mayıs 2023, ss.417-426
ive inherited prevalence ranging from 0.001% to 0.009% cases. It affects approximately
30% of LGMD patients and is therefore considered the most common subtype. It is a rare and
slowly progressive muscle disease caused by a mutation in the CAPN3 gene, which encodes
the proteolytic enzyme Calpain 3, a skeletal muscle-specific member of the Calpain family. In
the literature, the pathophysiological mechanisms involved in LGMDR1 are mostly unknown,
and there is no effective treatment for this disease to date. Currently, there is no comprehensive
study to understand the Calpain 3 protein. In this study, more than 7 bioinformatics tools such
as Expasy and HOPE were used to investigate the functional and structural states of proteins
caused by nsSNPs in the coding region of the human CAPN3 gene. The results have been
extensively studied with rational and semi-rational design approaches. All possible SNPs of
the gene, and the positions of the amino acids that make up the Calpain 3 protein produced by
this gene, were determined, as well as the effects of these positions. Some amino acid positions
have been highlighted as playing an active role in the stability of the protein structure, the
biological activity of the Calpain 3 protein, the preservation of the Calpain 3 protein structure,
and the interaction of the Calpain 3 protein with other proteins. Also, these amino asit positions
can change the physico-chemical properties of the Calpain 3 protein. These results are
supposed to be an important resource for studies on this protein and gene and will bring a
different perspective to the treatment studies designed for the disease