Extended Data Fig. 8: Results related with assembly intermediates.
From: Architecture and assembly mechanism of native glycine receptors
a, b, Representative FSEC profiles for recombinantly expressed homomeric GlyR tagged with YFP (a) and heteromeric GlyR tagged with CFP on β subunit (b), respectively. Melting temperatures (Tm) were determined by fitting the curves to a sigmoidal dose-response equation. c, A typical cryo-EM micrograph for recombinant GlyRs. The experiments were repeated three times with similar results. d, 2D class averages for recombinant GlyRs bound with 3D1 Fabs. e, f, Top down and side views for the recombinant heteromeric GlyR map, respectively. g, h, Top down and side views for the recombinant homomeric GlyR map, respectively. i, Side view of isolated α.B-α.C dimer from tetramer. Subunits are shown in cartoon representation. α.B and α.C are colored in blue and lime, respectively. The boxed areas are enlarged in panel (j) and (l). j, l, Superposition of the interfaces in the upper ECD (j) and the region near loop C (l) of α.B(+)/α.C(-) interface from homomeric α tetramer, heteromeric pentamer and homomeric pentamer. Orange arrows indicate the displacements of the Cα atoms. k, m, Schematic diagram illustrating the relative positions of the amino acids of the homomeric pentamer and tetramer. All distances are given in Å.
