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-Structure paper
タイトル | The structure of the native CNGA1/CNGB1 CNG channel from bovine retinal rods. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 29, Issue 1, Page 32-39, Year 2022 |
掲載日 | 2021年12月30日 |
著者 | Diane C A Barret / Gebhard F X Schertler / U Benjamin Kaupp / Jacopo Marino / |
PubMed 要旨 | In rod photoreceptors of the retina, the cyclic nucleotide-gated (CNG) channel is composed of three CNGA and one CNGB subunits, and it closes in response to light activation to generate an electrical ...In rod photoreceptors of the retina, the cyclic nucleotide-gated (CNG) channel is composed of three CNGA and one CNGB subunits, and it closes in response to light activation to generate an electrical signal that is conveyed to the brain. Here we report the cryo-EM structure of the closed state of the native rod CNG channel isolated from bovine retina. The structure reveals differences between CNGA1 and CNGB1 subunits. Three CNGA1 subunits are tethered at their C terminus by a coiled-coil region. The C-helix in the cyclic nucleotide-binding domain of CNGB1 features a different orientation from that in the three CNGA1 subunits. The arginine residue R994 of CNGB1 reaches into the ionic pathway and blocks the pore, thus introducing an additional gate, which is different from the central hydrophobic gate known from homomeric CNGA channels. These results address the long-standing question of how CNGB1 subunits contribute to the function of CNG channels in visual and olfactory neurons. |
リンク | Nat Struct Mol Biol / PubMed:34969975 |
手法 | EM (単粒子) |
解像度 | 3.4 Å |
構造データ | EMDB-12718, PDB-7o4h: |
由来 |
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キーワード | MEMBRANE PROTEIN / CNG channel / CNGA1 / CNGB1 / rod |