3SWY

CNGA3 626-672 containing CLZ domain

3SWY の概要

• エントリーDOI: 10.2210/pdb3swy/pdb
• 関連するPDBエントリー: 3SWF
• 分子名称: Cyclic nucleotide-gated cation channel alpha-3 (2 entities in total)
• 機能のキーワード: coiled-coil, assembly domain, transport protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Multi-pass membrane protein: Q16281
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 15740.90

構造登録者

Shuart, N.G.,Haitin, Y.,Camp, S.S.,Black, K.D.,Zagotta, W.N. (登録日: 2011-07-14, 公開日: 2011-09-14, 最終更新日: 2023-09-13)

主引用文献

Shuart, N.G.,Haitin, Y.,Camp, S.S.,Black, K.D.,Zagotta, W.N.
Molecular mechanism for 3:1 subunit stoichiometry of rod cyclic nucleotide-gated ion channels.
Nat Commun, 2:457-457, 2011

PubMed Abstract: Molecular determinants of ion channel tetramerization are well characterized, but those involved in heteromeric channel assembly are less clearly understood. The heteromeric composition of native channels is often precisely controlled. Cyclic nucleotide-gated (CNG) channels from rod photoreceptors exhibit a 3:1 stoichiometry of CNGA1 and CNGB1 subunits that tunes the channels for their specialized role in phototransduction. Here we show, using electrophysiology, fluorescence, biochemistry, and X-ray crystallography, that the mechanism for this controlled assembly is the formation of a parallel 3-helix coiled-coil domain of the carboxy-terminal leucine zipper region of CNGA1 subunits, constraining the channel to contain three CNGA1 subunits, followed by preferential incorporation of a single CNGB1 subunit. Deletion of the carboxy-terminal leucine zipper domain relaxed the constraint and permitted multiple CNGB1 subunits in the channel. The X-ray crystal structures of the parallel 3-helix coiled-coil domains of CNGA1 and CNGA3 subunits were similar, suggesting that a similar mechanism controls the stoichiometry of cone CNG channels.

PubMed: 21878911
DOI: 10.1038/ncomms1466

実験手法

X-RAY DIFFRACTION (1.9 Å)