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. 2005 Oct 10;102(42):15069–15074. doi: 10.1073/pnas.0505090102

Fig. 1.

Fig. 1.

Kinetic analyses of α9′ double mutants. (A) Locations of residues in the αε-subunit [Protein Data Bank ID code 2bg9 (28)]. Top to bottom: W149 is at the transmitter binding site, and S269(27′), V259(17′), and L251(9′) are in the M2 segment. The arrow (30 Å) marks approximately the membrane and the pore. (B) Continuous, low-time resolution view of currents from AChRs having a L9′T mutation in both α-subunits (inward current, down). Boxed cluster is shown at higher time resolution in C.(C) Clusters of openings from AChRs having different 9′ mutations in both α subunits. The WT residue (Leu) is boxed. (D) REFER plots for the α9′ double-mutant series. The solid line/filled symbols pertain to a membrane potential of –100 mV, and the dashed line/open symbols pertain to a membrane potential of +60 mV (see Fig. 7).