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.
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