Fig. 9: Conformation of Phe322 in xKCNQ1-CaM.
From: Structural and electrophysiological basis for the modulation of KCNQ1 channel currents by ML277
a Superposition of xKCNQ1-CaM and xKCNQ1-CaM-ML277 with hKCNQ1 (PDB-ID: 6V01), xKCNQ1 (PDB-ID: 5VMS), hKCNQ2 (PDB-ID: 7CR0) and hKCNQ4 (PDB-ID: 7VNQ, PDB-ID: 7BYL) structures showing detail around Phe322 (xKCNQ1) in a top view from the extracellular side. The previously published xKCNQ1-CaM and hKCNQ2 and hKCNQ4 structures show a corresponding Phe322 side-chain orientation pointing towards the ML277 binding site, while hKCNQ1 and our structures show a Phe322 oriented toward the pore. b Cryo-EM densities for Phe322 in xKCNQ1-CaM and xKCNQ1-CaM-ML277 (above) from this study, and from hKCNQ1 (F332, PDB-ID: 6V01) and xKCNQ1-CaM (Phe322, PDB-ID: 5VMS), below. The contour level cut offs were: maps from this study 8x rmsd, EMD-20967 6x rmsd, EMD-8712 1x rmsd.
