Crystal structure of channelrhodopsin, a light-gated cation channel - all cations lead through the monomer.

Crystal structure of channelrhodopsin, a light-gated cation channel - all cations lead through the monomer.
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DOI:
10.2142/biophysics.9.57
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发表时间:
2013
期刊:
Biophysics (Nagoya-shi, Japan)
影响因子:
--
通讯作者:
Nureki O
Nureki O
中科院分区:
其他
文献类型:
--
作者:
Kato HE;Nureki O

文献摘要

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通道视紫红质(Chr)是一种来源于绿藻的光门离子通道。由于阳离子的向内流动触发了神经元的放电,即使在自由运动的哺乳动物体内,表达CHRs的神经元也可以被光学控制。虽然CHR已广泛应用于神经科学研究,但对其分子机制知之甚少。我们测定了嵌合Chr的晶体结构,并揭示了它的分子结构。结构、电生理和计算分析的结合为了解CHR的通道功能提供了分子基础,并为具有新特性的CHR变体的原则性设计铺平了道路。
Channelrhodopsin (ChR) is a light-gated cation channel derived from green algae. Since the inward flow of cations triggers the neuron firing, neurons expressing ChRs can be optically controlled even within freely moving mammals. Although ChR has been broadly applied to neuro-science research, little is known about its molecular mechanisms. We determined the crystal structure of chimeric ChR at 2.3 Å resolution and revealed its molecular architecture. The integration of structural, electrophysio-logical, and computational analyses provided insight into the molecular basis for the channel function of ChR, and paved the way for the principled design of ChR variants with novel properties.