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. 2005 May 20;89(2):1020–1029. doi: 10.1529/biophysj.105.062240

FIGURE 3.

FIGURE 3

The 10-Å ring of methane molecules versus correolide and KvAP-based model of the Shaker channel. (A) Space-filled model of correolide viewed via the ring. (B) The side view of the Shaker model. The inner helices in two opposite domains are shown as ribbons. C-terminal parts of the pore helices and the selectivity-filter region are shown as rods. Correolide-sensing residues Ala-463, Val-467, Ala-471, Val-474, and Pro-475 are space-filled. Blue-colored Pro-475 at the cytoplasmic entrance is aligned with the 10-Å ring embracing correolide molecules in positions 0 through 8 Å from the ring plane (left). In the latter position (right), correolide would occur between the selectivity filter and the cytoplasmic entrance to the pore, which should be at least 10 Å wide to enable high-affinity binding of the drug. (C) Space-filled model of the KvAP-based model of the Shaker channel viewed via the 10-Å ring. Pro-473, Val-474, and Pro-475 are colored red, yellow, and green, respectively. Hydrogen atoms are not shown. Note a perfect match in the dimensions of the ring and the cytoplasmic entrance to the pore.