1VP6

M.loti ion channel cylic nucleotide binding domain

「1PF0」から置き換えられました

1VP6 の概要

• エントリーDOI: 10.2210/pdb1vp6/pdb
• 分子名称: Cyclic-nucleotide binding domain of mesorhizobium loti CNG potassium channel, BROMIDE ION, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: dimer helical bundle beta barrel core with cyclic amp bound, membrane protein
• 由来する生物種: Mesorhizobium loti
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: Q98GN8
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31100.58

構造登録者

Clayton, G.M.,Silverman, W.R.,Heginbotham, L.,Morais-Cabral, J.H. (登録日: 2004-10-14, 公開日: 2004-10-26, 最終更新日: 2023-12-27)

主引用文献

Clayton, G.M.,Silverman, W.R.,Heginbotham, L.,Morais-Cabral, J.H.
Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel.
Cell(Cambridge,Mass.), 119:615-627, 2004

PubMed Abstract: Here we describe the initial functional characterization of a cyclic nucleotide regulated ion channel from the bacterium Mesorhizobium loti and present two structures of its cyclic nucleotide binding domain, with and without cAMP. The domains are organized as dimers with the interface formed by the linker regions that connect the nucleotide binding pocket to the pore domain. Together, structural and functional data suggest the domains form two dimers on the cytoplasmic face of the channel. We propose a model for gating in which ligand binding alters the structural relationship within a dimer, directly affecting the position of the adjacent transmembrane helices.

PubMed: 15550244
DOI: 10.1016/j.cell.2004.10.030

実験手法

X-RAY DIFFRACTION (1.7 Å)