Structure-based DHHC-acyltransferase selectivity for fatty acids
Researchers from the Group of in silico analysis of membrane proteins structure and the Laboratory of biomolecular modeling IBCH RAS in collaboration with Russian and foreign colleagues have suggested the molecular basis of fatty acid selectivity in the human DHHC family of protein acyltransferases (hDHHC). Based on calculated large set of molecular dynamics simulations it was demonstrated that selectivity of hDHHC20 towards palmitoyl (C16) is predetermined by the teepee-like shape of the enzyme: there is a bottleneck in the middle of the transmembrane segment, that regulates the positioning of reacting groups of both molecules. This hypothesis enabled the prediction of the hDHHC20 mutant V185G with a presumed selectivity shift towards C18. The study is published in the International Journal of Molecular Sciences.
6 июня 2022 года