Gene Characterization, Molecular Docking and Dynamic Simulations of Insulin-Like Growth Factor Receptor (IGF-1Ra) in Common Carp, Cyprinus carpio

Insulin-like growth factors (IGF) are powerful mitogens for a wide range of cell types and play an essential role in growth and development. In the current study, molecular docking and structural analysis of Insulin-like growth factor receptors (IGF-1Ra), a tyrosine kinase receptor protein was performed. The outcomes revealed that IGF1Ra protein from C. carpio has nucleotide sequence of 5152 base pairs and open reading frame of 4224 base pairs with coding sequence (CDS) of 4224 that encodes 1407 amino acids (A.A). Protein structure validation and homology modeling of IGF-1Ra protein verify that the favored region contains 93.96% residues, while the allowed region contains 4.70% of amine acids. Through virtual screening of ligands and molecular docking, the maximum binding energy (− 8.8 kcal/mol) was observed in zinc sulphate heptahydrate ligand. Molecular interactions among different residues like ASN116, PRO35, LEU293 and PRO294 showed conventional hydrogen bonding. Subcellular localization and gene ontology revealed IGF-1Ra protein is utmost restricted in the nuclear region (42.1%) with score of 2.059 and ontology analysis indicated molecular function of 34.1%, biological process of 17.1% and cellular component of 23.2%. Phylogenetics and molecular evolutionary analysis showed IGF-1Ra protein is closely related to Labeo rohita and Danio rerio. Overall, the findings of present study may lead to the development of new molecules that may bind to the IGF-1Ra protein and will be helpful to stimulate fish growth. © 2023, Zoological Society, Kolkata, India.