Extended Data Fig. 7: Impact of the lipid bilayer on the structure of NTSR1. | Nature Structural & Molecular Biology

Extended Data Fig. 7: Impact of the lipid bilayer on the structure of NTSR1.

From: Cryo-EM structure of an activated GPCR–G protein complex in lipid nanodiscs

Extended Data Fig. 7

a, Comparison between the cryo-EM structures of the canonical states of NTSR1 (with Gi) in lipid bilayer (blue) and detergent (gray, PDB 6OS9). TM6 is shifted by 1.6 Å (based on Cα of V309) inwards in lipid bilayer. Right, comparison of the C-NTS-NTSR1-Gi-cND model (blue) with the density map of C-NTSR1-Gi-micelle (pink) (EMD-20180, low-pass filtered to 5 Å) confirms this shift to be significant. b, Structural comparison between the crystal structure of NTSR1 in detergent (green, PDB 4XEE) and the cryo-EM structure of the canonical state of NTSR1 in complex with Gi in detergent (gray, PDB 6OS9). The atomic models in (a) and (b) are superposed on NTSR1. c, Comparison of the localization of TM5-TM6 relative to α5-helix of Gα in class A GPCR-Gi complex structures, including the canonical state NTSR1 (blue) in complex with Gi (gold) structure reported in the current study, μOR-Gi (lime green; PDB 6DDE), Rho-Gi (hot pink; PDB 6CMO), A1R-Gi (cyan; PDB 6D9H), and CB1-Gi (purple; PDB 6N4B). The models are superposed on the Ras-like domain of Gα.

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