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. 2023 Jul 20;14:4368. doi: 10.1038/s41467-023-39262-2

Fig. 2. Conservation in the molecular design of Drosophila TMS1d, hSERINC3 structures and AlphaFold SERINC models, with location of hSERINC5 point mutants that abrogate restriction.

Fig. 2

a The Drosophila TMS1d monomer extracted from the cryoEM structure of the hexameric protein. b The WT hSERINC3 cryoEM model and map. c An AlphaFold model of hSERINC3 colored by pLDDT confidence score (blue, very high; cyan, high; yellow, low; orange very low). Low and very low-confidence loops were the same regions missing in the cryoEM maps and were removed for comparison. Backbone RMSDs for the TM domains were calculated in PyMOL. RMSDs are lower when aligning the TM bundles separately. d–f Vacuum electrostatic surface potentials for each model calculated in PyMOL demonstrating fairly similar electrostatic distributions for the three models (red, anionic and blue, cationic). Ribbon representation of AlphaFold 3D models for g hSERINC2 (gray), h hSERINC3 (gold), and i hSERINC5 (red). Point mutations in H8 and H9 are colored in cyan and boxed. j Closeup of (i) highlighting the hSERINC5-S328I mutation in H8 and the V396C and F397L mutations in H9 that abrogate restriction. (H1 was removed for clarity.).