Molecular modeling of a tandem two pore domain potassium channel reveals a putative binding site for general anesthetics.

Mutation of serine 155 to tryptophan or lysine 241 to alanine caused reductions in the LyTASK currents (Figure 6 A, Table 1 ); these reductions were not significant compared to wild-type (Figure 6 A, Table 1 ), but in the case of the S155W mutant there was a trend toward significance ( p = 0.06).

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