1N9P

Crystal Structure of the Cytoplasmic Domain of G-protein Activated Inward Rectifier Potassium Channel 1

Summary for 1N9P

• Entry DOI: 10.2210/pdb1n9p/pdb
• Descriptor: G protein-activated inward rectifier potassium channel 1 (2 entities in total)
• Functional Keywords: beta barrel, cytoplasmic domain, g protein, inward rectifier, potassium channel, metal transport
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 1
• Total formula weight: 23949.04

Authors

Nishida, M.,MacKinnon, R. (deposition date: 2002-11-26, release date: 2003-01-07, Last modification date: 2017-08-02)

Primary citation

Nishida, M.,MacKinnon, R.
Structural Basis of Inward Rectification: Cytoplasmic Pore of the G Protein-Gated Inward Rectifier GIRK1 at 1.8 A Resolution
Cell(Cambridge,Mass.), 111:957-965, 2002

PubMed Abstract: 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.

PubMed: 12507423
DOI: 10.1016/S0092-8674(02)01227-8

Experimental method

X-RAY DIFFRACTION (1.8 Å)