Protein-protein interactions themselves are frequently dependent or mediated by specific lipids in the membrane ( Barros et al., 2016 Munro, 2002) at the same time, they modify the local environment of the binding site to propagate a process or signaling cascade ( Monje-Galvan and Klauda, 2016 Sens et al., 2008 Stahelin, 2013). Protein-lipid interactions play key roles in cell growth, signaling processes, and disease onset and propagation ( Khan et al., 2016 Whited and Johs, 2015). Insertion events only occur with one of the membrane models, showing a combination of surface charge and internal membrane structure modulate this process. We characterized Myr insertion events from microsecond trajectories and examined the membrane response upon initial membrane targeting by MA. Our realistic membrane models confirm interactions with PIP 2 and PS lipids are highly favored around the HBR and are strong enough to keep the protein bound even without Myr insertion. Our study suggests Myr insertion is involved in the sorting of membrane lipids around the protein-binding site to prepare it for viral assembly. ![]() 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. We present a molecular dynamics simulation study on the binding mechanism of the membrane targeting domain of HIV-1 Gag protein. Specific protein-lipid interactions are critical for viral assembly.
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