Extended Data Fig. 8: Basis of α4β2 heteromeric assembly.
From: Structural principles of distinct assemblies of the human α4β2 nicotinic receptor
a, Cartoon representation of top view of observed (2α:3β and 3α:2β) and computational (4α:1β, 1α:4β, 5α and 5β) α4β2 pentameric assemblies. Assemblies on the top row (3α:2β, 4α:1β, and 5α) are arranged by increasing α4 composition. Assemblies on the bottom row (2α:3β, 1α:4β and 5β) are arranged by increasing β2 composition. Agonist binding sites are denoted by red circles. Buried interface areas (Å2) for the interfaces analysed in b, c are listed below each pentameric assembly. Subunits are coloured in a as described below for b, c. b, Superposition of α–α from 3α:2β and final α–α interface in 5α homopentamer. Principal subunits (grey) were superimposed to highlight differences at the interface. Complementary (−) subunits are coloured light green for α–α from 3α:2β and dark green for the α–α interface in the 5α homopentamer. Sticks are displayed for amino acid clashes that have greater than 1.5 Å overlap assessed by Molprobity. c, Superposition of the β–β interface from 2α:3β and final β–β interface in the 5β homopentamer. Principal subunits (grey) were superimposed to highlight differences at the interface. Complementary (−) subunits are coloured light blue for the β–β interface from the 2α:3β assembly and dark blue for the final β–β interface in the 5β homopentamer.
