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

TABLE 4.

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

Docking site DM490 DM497 PAM-4
TBE (kcal/mol) RMSD (VAR) TBE (kcal/mol) RMSD (VAR) TBE (kcal/mol) RMSD (VAR)
β+/α− (anesthetic)* −42 2.9 (0.1) −43 7.1 (0.1) −36 3.9 (0.2)
α+/β− (anesthetic) −38 5.1 (0.1) −38 11.3 (1.0) −38 13.9 (1.0)
γ+/β− (anesthetic) −35 5.7 (1.6) −39 4.9 (0.1) −32 12.4 (0.8)
α+/γ− (orphan) −41 17.5 (16.3) −40 8.0 (0.1) −29 4.1 (0.9)
Ion channel −40 3.7 (0.4) −34 11.1 (2.9) −27 5.2 (0.1)

TBE, theoretical binding energy (kcal/mol).

More negative values indicate higher binding affinity.

Depending on the RMSD VAR values, measured during the last third of the MDs, the observed interactions were considered stable (RMSD VAR < 0.2), nearly stable (RMSD VAR 0.2–2), and unstable (RMSD VAR > 2).

*Stable interaction within the (γ+)β+/α− interface.