Biomolecular Structural Rearrangement Analysis of FGFs Using Molecular Dynamics Simulations

Cellular and metabolic homeostasis is one of the vital physiological processes that are monitored and controlled by fibroblast growth factors, which also direct signaling pathways in living cells. In this paper, we attempted to envisage the glycine box, klotho protein, and the mechanism of biomolecular structural rearrangement of fibroblast growth factors. In silico molecular modeling and biomolecular dynamics simulations were employed to elucidate the structural rearrangements and mechanisms of activation of FGFs under defined physiological conditions, such as an aqueous or acidic environment. The molecular dynamics simulations revealed that the glycine box plays a crucial role in the catalysis of FGF19. The structural conformational changes observed in FGFs are due to the movement of His53, Lys55, and Phy142 amino acids and the β-sheet a part of the glycine box. There is a noticeable deletion of 32 residues (140–172) in the glycine box region of FGF19, as observed in the multiple sequence analysis of the FGF family that differentiates it. Researchers may be motivated by molecular movements of residues to create new inhibitors that can be used to cure cancer and maintain metabolic balance.