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. Author manuscript; available in PMC: 2013 Dec 27.
Published in final edited form as: Nature. 2013 Jun 5;498(7455):521–525. doi: 10.1038/nature12283

Figure 2. The pore properties of the p7(5a) channel.

Figure 2

a, The pore surface calculated using the program HOLE, showing the shape and constrictions of the pore. b, Sectional view of the channel showing the pore-lining residues with residues in red being strongly conserved. The numbers next to the helical segments represent the monomers to which the helices belong. c, A close view of the rings formed by Asn9 and Ile6 that constrict the N-terminal end of the channel. d, The current-voltage relationships of wildtype p7(2a) and the H9A and R35D mutants. Each data point is the mean ± SEM (standard error of mean) calculated over measurements from six different oocytes (n=6).