Fibroblast growth factor 5 FGF5 and its missense mutant FGF5 H174 underlying trichomegaly a molecular dynamics simulation investigation

Abstract
Introduction
Method
Protein retrieval and in silico mutagenesis
Molecular dynamics simulation setup
Construction of PCA free energy landscapes
Protein-protein docking and constructing residue interacting network
Visualization
Results
The missense mutation Y174H altered interactions with the solvent
The missense mutation Y174H decreased sheet and increased coil secondary structures
Decreased interaction of residue 174 with other residues was observed for H174
FGF5-H174 experienced more movement, instability, conformational changes
The mutation increased binding affinities towards FGFR1 with altered binding mode
Discussion
Disclosure statement
Funding
Orcid
References