Structural analysis and modeling comparison of primates dystrophin

Abstract

Dystrophin is a rod-shaped cytoplasmic protein which is an essential piece ofa protein complex that binds the cytoskeleton of a muscle fiber to the nearby extracellular matrix within the cell membrane. Lack of this protein in the muscle leads muscular dystrophy. Currently, Dystrophin structure has just been detected in human being. In fact, it has not been recognized in other types of primates. However, bioinformatics’ software has presented a big opportunity to predict its structure in other species on based on its structure in human being. The data for this project will be sourced by both bioinformatics databases and experimental information. The used databases were NCBI, PDB (protein data bank), UniProt, and Gene bank. The data that is gathered from these databases were analyzed using multiple sequence analysis software such as BLAST, Jalview to find conserved regions in the protein among the species of interest (different kinds of primates). In addition, the tertiary structure of the protein will be predicted by Swiss-model and will be observed and compared by 3-d structure viewing software such as: VMD and DeepView. In conclusion, the analysis of this study illustrates that Dystrophin has been changed slightly through evolution. However, the small changes that have been occurred have not affected the 3D structure and function of the protein.