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Figure 2.
Figure 2: The L483Y mutation and CTZ stabilize the GluR2 S1S2J
dimer. a, Side view of the S1S2J -L483Y dimer in complex with
AMPA. Subunit A is grey (domain 1) and blue (domain 2). Subunit
B is pink (domain 1) and purple (domain 2). Residues from A are
cyan; residues from B are yellow. Lys 505 and Ile 633 flank
transmembrane segments 1 and 2, respectively. b, Top view of the
L483Y dimer looking down the 2-fold axis. c, CTZ stabilizes the
GluR2 S1S2J -N754S dimer by binding in the dimer interface. Side
view of the S1S2J dimer in a complex with glutamate and CTZ. The
two CTZ molecules are green and are shown in CPK representation.
d, Top view of the S1S2J-Glu -CTZ dimer, looking down the 2-fold
axis. e, Interactions between Tyr 483 from one subunit and Leu
748 and Lys 752 from another subunit. Similar interactions also
occur in the dimer of S1S2J -L483Y in complex with DNQX. Note
the intersubunit hydrogen bond between Asn 754 and the carbonyl
oxygen of Ser 729. f, Interactions between CTZ and residues from
subunits A (cyan) and B (yellow). The black dashed lines are
hydrogen bonds and the light blue spheres are water molecules.
Stereoviews of e and f are provided in Supplementary Information.
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