Crystal Structure of Channelrhodopsin, A Light-Gated Cation Channel

• KATO Hideaki

  Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo

• NUREKI Osamu

  Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo

Bibliographic Information

Other Title

• 光駆動性陽イオンチャネルであるチャネルロドプシンの結晶構造
• ヒカリ クドウセイ ヨウ イオンチャネル デ アル チャネルロドプシン ノ ケッショウ コウゾウ

Abstract

Channelrhodopsin (ChR) is a light-gated cation channel derived from algae that conducts cations, including sodium ions, in a light-dependent manner. Because the inward flow of sodium ions triggers the neuron firing, neurons expressing ChRs can be optically controlled even within freely moving mammals. Although ChR has been broadly applied to neuroscience research, little is known about its molecular mechanisms. We determined the crystal structure of ChR at 2.3 Å resolution and revealed its molecular architecture, especially, the cation-conducting pathway. The integration of structural and electrophysiological analyses provided insight into the molecular basis for the remarkable function of ChR, and paved the way for the principled design of ChR variants with novel properties.

Journal

• Nihon Kessho Gakkaishi

  Nihon Kessho Gakkaishi 54 (4), 220-225, 2012

  The Crystallographic Society of Japan

Details

• CRID: 1390282679066949504
• NII Article ID: 10031042484
• NII Book ID: AN00188364
• DOI: 10.5940/jcrsj.54.220
• ISSN: 18845576
• ISSN: 03694585
• NDL BIB ID: 023970077
• Web Site: http://id.ndl.go.jp/bib/023970077
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I023970077
• Text Lang: ja
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed