Extended Data Fig. 6: Lipid screening.
From: A bipartite structural organization defines the SERINC family of HIV-1 restriction factors
a, Lipid binding groove apparent in DmSERINC structure. Top left, Surface representation of DmSERINC monomer revealing a groove formed between TMs 5, 7, 8, and 4. Top right, Lipid moiety modeled into the groove, shown in spheres, illustrating complementary size, shape, and location for lipid binding. Bottom left, Cartoon representation of the same view with helices labeled and colored as Fig. 1b. Bottom right, Cartoon representation with lipid shown in stick format. b, Cryo-EM map has lipid-like features in this groove. Left, map with PS modeled in. Right, Map carved to 2.5 Å around the modeled PS to highlight the lipid-like map features. c, View of DmSERINC in a POPC membrane, after 215 ns of atomistic simulation. The protein is shown as a blue cartoon and transparent surface, and the POPC lipids are red, orange, and gray spheres. Lipids in front of the protein have been removed to reveal how the protein sits in the membrane. d, View of DmSERINC after 215 ns atomistic MD simulation, showing a POPC lipid bound to the groove between TM5 and TM8. The protein is shown as a white cartoon, with the lipid in green, red, and gold spheres. Note that this lipid remains bound for the full simulation. e−g, Lipid thermostability assay. e, Change in thermostability of DmSERINC hexamer upon the addition of a specific lipid. f, Change in thermostability of DmSERINC monomer upon the addition of a specific lipid. g, Change in thermostability of SERINC5 upon the addition of a specific lipid (selected sample of lipids). Data shown in e,f are mean and s.d. of n = 3−6 technical replicates. Data are provided in Source Data.
