Molecular basis for Kir6.2 channel inhibition by adenine nucleotides Biophysical Journal | January 1, 2003| | Copyright Biophysical Society Jan 2003. Provided by ProQuest LLC. (Hide copyright information) Copyright

ABSTRACT K^sub ATP^ channels are comprised of a pore-forming protein, Kir6.x, and the sulfonylurea receptor, SURx. Interaction of adenine nucleotides with Kir6.2 positively charged amino acids such as K185 and R201 on the C-terminus causes channel closure. Substitution of these amino acids with other positively charged residues had small effects on inhibition by adenine nucleotide, while substitution with neutral or negative residues had major effects, suggesting electrostatic interactions between Kir6.2 positive charges and adenine nucleotide negative phosphate groups. Furthermore, R201 ...

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