Fig. 3: Outer leaflet phospholipid binding site and conformational changes associated with ELIC opening. | Nature Communications

Fig. 3: Outer leaflet phospholipid binding site and conformational changes associated with ELIC opening.

From: Open-channel structure of a pentameric ligand-gated ion channel reveals a mechanism of leaflet-specific phospholipid modulation

Fig. 3

a Left: Structure of ELIC5 TMD viewed from extracellular side showing bound POPG (yellow) in the density map (green). Right: Side view of ELIC5 phospholipid binding site showing POPG (yellow) in the density map (green). The R117 side chain is shown. b Phospholipid density (red) displayed at σ-level of 3.0 from cryo-EM density maps of WT apo, WT CA, and ELIC5 CA. c Top: Conformational changes in the β6-β7 loop and the M2-M3 linker in WT apo, WT CA and ELIC5 CA. Shown is the W206 side chain for each structure. Bottom: Top down view of the conformational changes of the M2-M3 linker and W206 of WT apo, WT CA and ELIC5 CA. d View of the TMD helices from the extracellular side at the level of 9’ comparing WT CA and ELIC5 CA. Distances between C-α carbons of each structure are shown in red for each transmembrane helix. Images are from a global superposition of structures.

Back to article page