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. Author manuscript; available in PMC: 2016 Nov 18.
Published in final edited form as: Nature. 2016 May 18;534(7607):347–351. doi: 10.1038/nature17964

Figure 2. Structural details of tripartite toxin-channel-lipid complex.

Figure 2

a, Sequence of DkTx (top) showing location of intramolecular disulfide bonds and finger-like loops formed primarily by residues conserved between toxin knots (orange). Hydrophobic residues enable fingers to penetrate the lipid bilayer by ~9Å (bottom). b, Schematic top down view showing antiparallel arrangement of two DkTx molecules (purple) binding at subunit interfaces of a TRPV1 homo-tetramer (subunits are color-coded). c, Cutaway view depicting one DkTx molecule interacting with two adjacent TRPV1 subunits (grey) and associated lipids (blue spheres; red and orange spheres depict phosphate head groups). Superimposed ribbon diagram (light blue) denotes location of transmembrane α-helices for one channel subunit. d, Detailed view of boxed region in (c) showing interactions between lipids and amino acid side chains from channel and toxin (dotted line, hydrogen bond). Helices from three neighboring channel subunits are color-coded as in (b).