Journal
CELL
Volume 111, Issue 7, Pages 957-965Publisher
CELL PRESS
DOI: 10.1016/S0092-8674(02)01227-8
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Inward rectifier K+ channels govern the resting membrane voltage in many cells. Regulation of these ion channels via G protein-coupled receptor signaling underlies the control of heart rate and the actions of neurotransmitters in the central nervous system. We have determined the protein structure formed by the intracellular N- and C termini of the G protein-gated inward rectifier K+ channel GIRK1 at 1.8 Angstrom resolution. A cytoplasmic pore, conserved among inward rectifier K+ channels, extends the ion pathway to 60 Angstrom, nearly twice the length of a canonical transmembrane K+ channel. The cytoplasmic pore is lined by acidic and hydrophobic amino acids, creating a favorable environment for polyamines, which block the pore. These results explain in structural and chemical terms the basis of inward rectification, and they also have implications for G protein regulation of GIRK channels.
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