Fig. 9: Key conformations of the ΔASIC1/JNJ-799760 complex. | Communications Biology

Fig. 9: Key conformations of the ΔASIC1/JNJ-799760 complex.

From: Molecular mechanism and structural basis of small-molecule modulation of the gating of acid-sensing ion channel 1

Fig. 9

a Superposition of ΔASIC1/JNJ-799760 (colored by domain) and 3S3W apo (gray/transparent) structures. Binding of JNJ-799760 causes outward pivots of α4 and α5 (split into α5a and α5b) and displacement of the acidic loop. b Superposition of ΔASIC1/JNJ-799760 (green) and 3S3W (gray/transparent) near the acidic pocket. Note the increased side-chain distance of D238–D350 and of E239–D346. Numbers are in Å. Note that E239 and Y341 side chains in 3S3W clash with JNJ-799760. c Superposition of ΔASIC1/JNJ-799760 (green) and 3S3W (gray) for a portion of the β1–β2 linker. Note the ~180° flip of the T84–R85 peptide bond orientation. d Superposition of ΔASIC1/JNJ-799760 (green) and 3S3W (gray) for a portion of the β11–β12 linker. Note the swap of L414–N415 side-chain orientations and displacements of L414 and β11–β12 linker due to JNJ-799760 binding. e Comparison of chain A TM domains of ΔASIC1/JNJ-799760 (green) and 3S3W (gray). Note the extended GAS belt conformation and TM2b domain swap in ΔASIC1/JNJ-799760.

Back to article page