1U4E

Crystal Structure of Cytoplasmic Domains of GIRK1 channel

1U4E の概要

• エントリーDOI: 10.2210/pdb1u4e/pdb
• 関連するPDBエントリー: 1N9P 1P7B
• 分子名称: G protein-activated inward rectifier potassium channel 1 (2 entities in total)
• 機能のキーワード: 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: 24152.57

構造登録者

Pegan, S.,Arrabit, C.,Zhou, W.,Kwiatkowski, W.,Slesinger, P.A.,Choe, S. (登録日: 2004-07-24, 公開日: 2005-03-08, 最終更新日: 2023-08-23)

主引用文献

Pegan, S.,Arrabit, C.,Zhou, W.,Kwiatkowski, W.,Collins, A.,Slesinger, P.A.,Choe, S.
Cytoplasmic domain structures of Kir2.1 and Kir3.1 show sites for modulating gating and rectification
Nat.Neurosci., 8:279-287, 2005

PubMed Abstract: N- and C-terminal cytoplasmic domains of inwardly rectifying K (Kir) channels control the ion-permeation pathway through diverse interactions with small molecules and protein ligands in the cytoplasm. Two new crystal structures of the cytoplasmic domains of Kir2.1 (Kir2.1(L)) and the G protein-sensitive Kir3.1 (Kir3.1(S)) channels in the absence of PIP(2) show the cytoplasmic ion-permeation pathways occluded by four cytoplasmic loops that form a girdle around the central pore (G-loop). Significant flexibility of the pore-facing G-loop of Kir2.1(L) and Kir3.1(S) suggests a possible role as a diffusion barrier between cytoplasmic and transmembrane pores. Consistent with this, mutations of the G-loop disrupted gating or inward rectification. Structural comparison shows a di-aspartate cluster on the distal end of the cytoplasmic pore of Kir2.1(L) that is important for modulating inward rectification. Taken together, these results suggest the cytoplasmic domains of Kir channels undergo structural changes to modulate gating and inward rectification.

PubMed: 15723059
DOI: 10.1038/nn1411

実験手法

X-RAY DIFFRACTION (2.09 Å)