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. Author manuscript; available in PMC: 2019 Oct 26.
Published in final edited form as: Science. 2019 Apr 11;364(6438):355–362. doi: 10.1126/science.aaw8250

Fig. 4. ATD layer and ATD-LBD interface.

Fig. 4

(A-C) Capital ‘Y’ view of di-heteromeric A1A2A1A2 (A), A3A2A3A2 (B) or tri-heteromeric A1A2A3A2 complexes (C). The COM distances between the ATD and LBD layers, and between the LBD and TMD layers, are shown. The spaces between the ATD and LBD layers are indicated by a square bracket. A’-C’ and B’-D’ auxiliary proteins are grey and green. (D) ATD layer analysis of the A1A2A1A2 and A3A2A3A2 complexes. The ATD model of the A1A2A1A2 complex is in the left panel, in which the COMs of the R1 and R2 lobes are indicated by black dots. The distances and angles of vectors defined by COMs of the A1A2A1A2 (upper right) or the A3A2A3A2 (lower right) complex are shown in the right two panels. (E) Interactions that may stabilize the ATD dimer-dimer interface. ‘Top’ view of the ATD layer of the A3A2A3A2 complex is in the left panel. Boxed regions in the right panels highlight dimer-dimer contacts, viewed parallel or perpendicular to the overall 2-fold axis. The α7 helix is colored from blue at the N-terminus to red at the C-terminus. His 208 and N-linked carbohydrates are in ‘sticks’. (F-G) ATD-LBD interface comparison between GluA1 and GluA3 subunits from A1A2A1A2 and A3A2A3A2 complexes or from the A1A2A3A2 complex. Structures were superimposed using the LBD layer. COMs of the D1 lobe, GluA1 R1/R2 lobes and GluA3 R1/R2 lobes are indicated by black, blue and orange dots. Distances are in ängstroms (Å).