Fig. 2
From: Cryo-EM reveals ligand induced allostery underlying InsP3R channel gating
Structural rearrangements in the ligand-binding pocket of InsP3R1. a Shown is an overlay of ribbon diagrams of the ARM1 and β-TF2 domains from Apo-InsP3R1 (light purple) and AdA-InsP3R1 (green). The structure of AdA molecule is colour-coded by element (phosphorous - orange; oxygen - red; nitrogen - blue; carbon - grey) and shown within the binding pocket; 2′-, 3′′- and 4′′- phosphates are labeled. Distances between Cα atoms at the narrowest point within the ligand binding pocket for AdA-bound (between T266 and K569) and Apo-InsP3R1 (between G268 and K569) are indicated. b Overlay of the AdA- (green) and Apo- (light purple) InsP3R1 structures zoomed in at the β-TF1/β-TF2′ interface. Y167 is depicted as a sphere. c The Cα RMS deviations calculated between Apo- and AdA-bound structures are shown in the AdA-bound LBD structure colour-coded based on RMS deviation - ribbon color/thickness denotes lowest RMSD (blue/thinnest) to highest RMSD (orange/thickest). The most variable residues contributing to intra- and inter-domain contacts are labeled. Wide arrows point to the interacting domains of neighboring subunits. The prime symbol (′) is used to differentiate subunits
