1N9P

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

1N9P の概要

• エントリーDOI: 10.2210/pdb1n9p/pdb
• 分子名称: G protein-activated inward rectifier potassium channel 1 (2 entities in total)
• 機能のキーワード: beta barrel, cytoplasmic domain, g protein, inward rectifier, potassium channel, metal transport
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23949.04

構造登録者

Nishida, M.,MacKinnon, R. (登録日: 2002-11-26, 公開日: 2003-01-07, 最終更新日: 2017-08-02)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.8 Å)