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. Author manuscript; available in PMC: 2014 Jul 15.
Published in final edited form as: Structure. 2013 Feb 21;21(3):414–425. doi: 10.1016/j.str.2013.01.006

Figure 7.

Figure 7

Crystal structure and functional analysis of the AvGluR1 LBD dimer assembly. (A and B) The AvGluR1 dimer has an ‘upright’ orientation compared to the GluA2 dimer; α-Helix H and its symmetry mate in AvGluR1, and α-helix J and its symmetry mate in GluA2, are drawn as transparent cylinders; the angle between vectors running through the center of these helices is 45° in AvGluR1 and 61° in GluA2. (C) Stereoview of the AvGluR1 LBD dimer assembly viewed parallel to the dimer interface formed by α-helices C and H, with a ribbon diagram for subunits colored gold and rose; side chains mediating salt bridges and polar interactions are drawn as sticks connected by dashed lines; chloride ions are drawn as spheres; Leu766 is located in the lower third of α-helix H. (D) Desensitization is abolished by the S520C/L766C mutation; the left panel shows a control response to 100 μM glutamate recorded from wild type AvGluR1, with the onset of desensitization fit with a single exponential of time constant 460 ms; the next three panels show responses to 100 μM glutamate recorded from one oocyte for the AvGluR1 S520C/L766C mutant before, during, and 20 min after application of 10 mM DTT for 5 min.