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- W1999217967 abstract "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 × 200 × 235 Å. This large dimension of TRPC3 is also supported by the Stokes radius (92 Å) obtained from gel filtration chromatography." @default.
- W1999217967 created "2016-06-24" @default.
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- W1999217967 date "2005-08-01" @default.
- W1999217967 modified "2023-10-15" @default.
- W1999217967 title "The non-selective cation-permeable channel TRPC3 is a tetrahedron with a cap on the large cytoplasmic end" @default.
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- W1999217967 doi "https://doi.org/10.1016/j.bbrc.2005.05.181" @default.
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