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. 2012 Nov;140(5):495–511. doi: 10.1085/jgp.201210823

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© 2012 Goodchild et al.

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Figure 8. — Docking of large intracellular cations within the inner cavity of the crystal structure of the Kv1.2 open pore. (A and B) A cutaway view of the pore (S5–S6) of Kv1.2, with one subunit of the tetramer cut away for viewing with TEA⁺ (A) or NMG⁺ (B; carbon atoms are colored green) ions docked deep in the inner cavity of the channel. (bottom) Close up of binding pocket. Residues forming the binding pocket (defined as within 4 Å of the ligand) are displayed as sticks (carbon atoms are yellow). (Images were generated with PyMol.) Residues within a 4-Å radius were as follows: the intracellular cavity facing V399 and I402 in S6, and T373 and T374 at the intracellular entrance to the selectivity filter. I402 is labeled. The interaction of the ligands with both polar and aliphatic residues suggested a mixed contribution of hydrophobic and electrostatic contributions to the binding.