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. 2006 Jul 28;91(8):2860–2873. doi: 10.1529/biophysj.105.080242

FIGURE 5.

FIGURE 5

(A) Representative conformations of the TM domain of one subunit of the Kir3.4*G175K mutant showing the interactions observed between K175 and the side chain of N179 and (B) the side chain of T149, which is a part of the selectivity filter. The inserts display the details of the nomenclature of the atoms that participate in the interaction. (C) Whole-cell basal currents from Kir3.4*, Kir3.4*N179D, Kir3.4*G175D, Kir3.4*G175E, Kir3.4*G175K, Kir3.4*G175Q and the double mutants Kir3.4*G175D_N179D, Kir3.4*G175E_N179D, Kir3.4*G175K_N179D, and Kir3.4*G175Q_N179D recorded in Xenopus oocytes at −80 mV. (D) Confocal images from oocyte sections expressing GFP-tagged Kir3.4* subunits or Kir3.4*G175K. An image from an uninjected oocyte section is shown for comparison. Black and white images of the oocyte sections are also shown. (E) Examples of single channel bursts obtained from Kir3.4*, Kir3.4*N179D, Kir3.4*G175D, Kir3.4*G175E, Kir3.4*G175K, and Kir3.4*G175Q recorded at −80 mV in a cell-attached mode.