视网膜环鸟苷酸门控通道的分子结构：胞质结构域的排列
Molecular architecture of a retinal cGMP-gated channel: the arrangement of the cytoplasmic domains.
作者信息
Higgins Matthew K, Weitz Dietmar, Warne Tony, Schertler Gebhard F X, Kaupp U Benjamin
机构信息
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
出版信息
EMBO J. 2002 May 1;21(9):2087-94. doi: 10.1093/emboj/21.9.2087.
Abstract
Cyclic nucleotide-gated (CNG) channels play a central role in the conversion of sensory information, such as light and scent, into primary electrical signals. We have purified the CNG channel from bovine retina and have studied it using electron microscopy and image processing. We present the structure of the channel to 35 A resolution. This three-dimensional reconstruction provides insight into the architecture of the protein, suggesting that the cyclic nucleotide-binding domains, which initiate the response to ligand, 'hang' below the pore-forming part of the channel, attached by narrow linkers. The structure also suggests that the four cyclic nucleotide-binding domains present in each channel form two distinct domains, lending structural weight to the suggestion that the four subunits of the CNG channels are arranged as a pair of dimers.
摘要
环核苷酸门控（CNG）通道在将光和气味等感觉信息转化为初级电信号的过程中起着核心作用。我们已从牛视网膜中纯化出CNG通道，并利用电子显微镜和图像处理技术对其进行了研究。我们展示了该通道分辨率达35埃的结构。这一三维重建为该蛋白质的结构提供了深入见解，表明引发对配体反应的环核苷酸结合结构域通过狭窄的连接子附着在通道成孔部分下方“悬挂”着。该结构还表明，每个通道中存在的四个环核苷酸结合结构域形成两个不同的结构域，这为CNG通道的四个亚基以一对二聚体形式排列的观点提供了结构上的支持。
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