1n9p
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Crystal Structure of the Cytoplasmic Domain of G-protein Activated Inward Rectifier Potassium Channel 1
OverviewOverview
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 A resolution. A, cytoplasmic pore, conserved among inward rectifier K(+) channels, extends, the ion pathway to 60 A, 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.
About this StructureAbout this Structure
1N9P is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of inward rectification: cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 A resolution., Nishida M, MacKinnon R, Cell. 2002 Dec 27;111(7):957-65. PMID:12507423
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