Fig. 5: Ligand-dependent structural reorganization of Lys301.
From: Structural insights into the allosteric inhibition of P2X4 receptors
a–c Close-up views of the allosteric site of zfP2X4, viewed from the extracellular side, are shown in surface representations. a The zfP2X4 structure in the apo state (PDB ID: 4DW0). b The BX430-bound zfP2X4 structure (this study). c The BAY-1797-bound zfP2X4 structure (this study). d–g Allosteric sites of zfP2X4 in the apo structure (PDB ID: 4DW0) (d, e), in the BX430-bound structure (f), and in the BAY-1797 bound structure (g). The BX430 (f) and BAY-1797 (g) molecules are shown in sphere representation. The BX430 molecule from the BX430-bound structure superposed onto the apo structure is shown in half-transparent sphere representation (d, e). h, i MD simulations of the BX430-bound structure (h) and the BAY-1797-bound structure (i). Distance plots between the NZ atom of Lys301 and the center of the aromatic ring of Tyr302. The averaged distance values from the three subunits of the trimer are shown. Two more additional repeats of the MD simulations were shown in Supplementary Fig. 13M–P. In total, MD simulations were performed three times.
