3ATA
Crystal Structure of the Kir3.2 Cytoplasmic Domain (Na+-free crystal soaked in 10 mM barium chloride and 10 mM Spermine)
3ATA の概要
エントリーDOI | 10.2210/pdb3ata/pdb |
関連するPDBエントリー | 2e4f 3AT8 3AT9 3ATB 3ATD 3ATE 3ATF 3agw |
分子名称 | Potassium inwardly-rectifying channel, subfamily J, member 6, BARIUM ION (2 entities in total) |
機能のキーワード | cytoplasmic assembly, beta-barrel, ion transport, g protein beta-gamma subunits, transport protein |
由来する生物種 | Mus musculus (mouse) 詳細 |
細胞内の位置 | Membrane ; Multi-pass membrane protein : Q0VB45 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 23886.32 |
構造登録者 | |
主引用文献 | Inanobe, A.,Nakagawa, A.,Kurachi, Y. Interactions of cations with the cytoplasmic pores of inward rectifier K(+) channels in the closed state J.Biol.Chem., 286:41801-41811, 2011 Cited by PubMed Abstract: Ion channels gate at membrane-embedded domains by changing their conformation along the ion conduction pathway. Inward rectifier K(+) (Kir) channels possess a unique extramembrane cytoplasmic domain that extends this pathway. However, the relevance and contribution of this domain to ion permeation remain unclear. By qualitative x-ray crystallographic analysis, we found that the pore in the cytoplasmic domain of Kir3.2 binds cations in a valency-dependent manner and does not allow the displacement of Mg(2+) by monovalent cations or spermine. Electrophysiological analyses revealed that the cytoplasmic pore of Kir3.2 selectively binds positively charged molecules and has a higher affinity for Mg(2+) when it has a low probability of being open. The selective blocking of chemical modification of the side chain of pore-facing residues by Mg(2+) indicates that the mode of binding of Mg(2+) is likely to be similar to that observed in the crystal structure. These results indicate that the Kir3.2 crystal structure has a closed conformation with a negative electrostatic field potential at the cytoplasmic pore, the potential of which may be controlled by conformational changes in the cytoplasmic domain to regulate ion diffusion along the pore. PubMed: 21982822DOI: 10.1074/jbc.M111.278531 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.49 Å) |
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