Insights into Evolutionary and Conservancy Analytics on Human Insulin Receptor Proteins

Background: The insulin receptor protein of humans is proposed to have substantial application in the regulatory pathway of glucose levels in the blood. The cellular function of the insulin hormone is initiated by its association with the insulin receptor (IR) protein, and this process is common to most vertebrate species. Thus, phylogenetic analysis of IR protein among various associated species in vertebrates can elucidate the importance of residues and structure, and the relationship with its function as the conserved region of residues is associated with evolutionary conservation on insulin receptor proteins. In the present study, we have used various in silico approaches and conducted the phylogenetic analysis. Methods: The basic local alignment search tool (BLAST) was employed to screen the 250 vertebrates. After evolutionary analysis, Pan troglodytes (Chimpanzees) have been observed as the closest relatives of Homo sapiens concerning insulin receptor proteins. Results: Human insulin receptor protein was found to have hydrophobic nature by hydrophobicity profile analysis, where most of the positions were above the mean hydrophobicity value from n-terminal to cterminal residues, whereas carboxy-terminal residues were observed as hydrophilic. High entropy was observed at the short stretch at N-terminal, C-terminal, and a linker region within the alignment, but the overall positions which were aligned showed low entropic regions. Conclusion: The outcomes of this work have revealed some unexplored specific characteristics of the conserved domains among different taxa of selected vertebrates and have also illustrated the hierarchical assemblage-based inconsistent variation of the IR proteins, and further conservancy analysis discloses the significance of each site for protein structure or function.