Binding mechanism of the matrix domain of HIV-1 gag on lipid membranes.

ABSTRACT: Specific protein-lipid interactions are critical for viral assembly. We present a molecular dynamics simulation study on the binding mechanism of the membrane targeting domain of HIV-1 Gag protein. The matrix (MA) domain drives Gag onto the plasma membrane through electrostatic interactions at its highly-basic-region (HBR), located near the myristoylated (Myr) N-terminus of the protein. Our study suggests Myr insertion is involved in the sorting of membrane lipids around the protein-binding site to prepare it for viral assembly. Our realistic membrane models confirm interactions with PIP₂ and PS lipids are highly favored around the HBR and are strong enough to keep the protein bound even without Myr insertion. We characterized Myr insertion events from microsecond trajectories a

SUBMITTER: Monje-Galvan V 

PROVIDER: S-EPMC7476761 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature