Figure 2 - full size

 

Figure 2.
Figure 2: Structure of NR1-NR2A S1S2. a, Side view of the NR1-NR2A S1S2 heterodimer in complex with glycine and glutamate. NR1 and NR2A are coloured green and blue, respectively. Glycine, glutamate and the C atom of the glycine residue in the Gly-Thr dipeptide linker are shown as spheres. The arrow indicates the pseudo two-fold axis between the protomers. b, View of the structure from the 'top'. The interface between NR1 and NR2A is sliced into three sections denoted sites I-III. c-e, Magnified view of the interactions at sites I, II and III. Dashed lines indicate hydrogen bonds or salt bridges. The interacting residues from NR1 and NR2A are coloured white and orange, respectively. f, g, Structural comparison between the NR1-NR2A (green-blue) S1S2 heterodimer and the glutamate-bound GluR2 S1S2 (pink) homodimer (PDB code 1FTJ). Superimposed structures are viewed from the side and 'top' of the molecules in f and g, respectively. Superposition was carried out on 256 residues from domain 1 with the program LSQKAB^50. The C atoms of the glycine residues in the Gly-Thr dipeptide linkers are shown as spheres.

The above figure is reprinted by permission from Macmillan Publishers Ltd: Nature (2005, 438, 185-192) copyright 2005.