2005年8月
The non-selective cation-permeable channel TRPC3 is a tetrahedron with a cap on the large cytoplasmic end
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
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- 巻
- 333
- 号
- 3
- 開始ページ
- 768
- 終了ページ
- 777
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.bbrc.2005.05.181
- 出版者・発行元
- ACADEMIC PRESS INC ELSEVIER SCIENCE
TRPC3 plays important roles in neuronal differentiation and immune cell maturation by mediating the cationic current in response to phospholipase C activation, Ca2+ depletion, and diacylglycerol stimulation. Here, we purified the TRPC3 channel using a glycosylated tetramer and observed the structure using electron microscopy. Negatively stained specimens demonstrate homogeneous protein particles containing an internal cavity-like structure. These particle images were picked up by automated pick-up programs, aligned, and classified by the growing neural gas network method. Similarly oriented projections were averaged to decrease the signal-to-noise ratio. The averaged images progress from the top view to the side views, which are representative of their raw images. The top view confirmed the hypothesis of a four-domain structure, and the side view demonstrates a large cytoplasmic domain with a capped structure at the bottom, which is near a predicted locus of ion release. The total image of the protein is a blunt-edged trapezoid of 200 x 200 x 235 angstrom. This large dimension of TRPC3 is also supported by the Stokes radius (92 A) obtained from gel filtration chromatography. (c) 2005 Elsevier Inc. All rights reserved.
- リンク情報
- ID情報
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- DOI : 10.1016/j.bbrc.2005.05.181
- ISSN : 0006-291X
- Web of Science ID : WOS:000230418800016