Fig. 1: Structures of human PANX1.
From: Structural basis for gating mechanism of Pannexin 1 channel
a Overall structure of human PANX1. Left, extracellular view; middle, side view; right, the surface electrostatic potential of PANX1 calculated by PyMOL. b Structural comparison between PANX1ΔCT and full-length PANX1. Full-length PANX1 and PANX1ΔCT are shown in cartoon and colored rainbow and gray, respectively. c The pore and pore radius of PANX1. Surface representation of the central pore of PANX1 (left panel); the pore radius of PANX1 was calculated by HOLE (right panel). d The narrowest constrictive site in the extracellular region. The key residues W74 and R75 are shown as spheres (left panel). Another constrictive site in the extracellular region, I58, is shown as spheres (right panel). e Interactions between two extracellular domains of PANX1. The residues in the interface of the two protomers are shown as sticks. f Intracellular constrictive site of PANX1. The key residues, T21/E22/P23, are shown as spheres. g Locations of gain-of-function mutations and posttranslational modification sites. The key helices are colored orange in the heptamer (left panel). K346 and C347 are shown as sticks. The phosphorylation site Y309 is colored purple.
