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. 2023 Sep;104(3):115–131. doi: 10.1124/molpharm.123.000692

TABLE 5.

Molecular interactions of DM490, DM497, and PAM-4 at the subunit interfaces and ion channel of the α1β2γ2 GABAAR model

DM490 DM497 PAM-4
Intersubunit Sites
Docking Site (+) side (−) side (+) side (−) side (+) side (−) side
β/α (A) TM2: M261 T262 N265
TM3: L285 M286 F289
V290
TM1: I228
Q229 L232
P233 M236
TM2: T262 N265
TM3: D282 L285 M286
F289 V290
TM1: I228
Q229 L232
P233 M236
TM2: M261 T262 N265
TM3: L285 M286 F289
V290
TM1: I228
N229 L232
P233 M236
α/β (A) TM2: T267 S270
TM3:A283 D287 W288 I290
A291 Y294
TM1: L223
M227 P228
L231
Near stable Near stable
γ/β (A) Near stable TM2: T277 S280
TM3: S301 F304 I305
F308
TM1: L223
Q224 M227
P228 L231
Near stable
α/γ (O) Unstable TM2: S270
TM3: D287 I290 A291
Y294 A295 F298 S299 I302
TM1: I238
I242 L246
Near stable
Ion Channel Site
γ subunit Not found Not found TM2: L274 (9’), T277, T278 (13’)
β subunit Near stable Unstable TM1: I232
TM2: I255, T256, L259 (9’),
T260, T263 (13’), I264
α subunit TM2: T261 (6’), T265

A, anesthetic site; O, orphan site.

The “+” and “−” sides indicate contributions made by the two sides of an intersubunit interface within a counterclockwise order of subunits.

Residues in bold: π-π interactions.

Residues at 6’, 9’, and 13’ correspond to the canonical TM2 rings in the ion channel lumen.