Abstract
The inositol 1,4,5-trisphosphate receptor (IP 3 R) is a tetrameric intracellular Ca 2+ channel, which mediates the release of Ca 2+ from the endoplasmic reticulum in response to many different extracellular stimuli. We present a 3D structure of the type 1 IP 3 R obtained by electron microscopy and single-particle analysis that reveals its domain organization. The IP 3 R has a flower-like appearance with fourfold symmetry and is made up of three distinct domains connected by slender links. By relating the organization of the structural domains to secondary-structure predictions and biochemical data we develop a model in which structural domains are mapped onto the amino acid sequence to deduce the location of the channel region and the cytoplasmic inositol 1,4,5-trisphosphate-binding and modulatory subdomains. The structure of the IP 3 R is compared with that of other tetrameric cation channels. The channel domain is similar in size and shape to its counterparts in the ryanodine receptor and the Shaker voltage-gated K + channel.
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Dates
Type | When |
---|---|
Created | 22 years, 4 months ago (April 1, 2003, 2:25 p.m.) |
Deposited | 3 years, 4 months ago (April 25, 2022, 10:05 p.m.) |
Indexed | 11 months, 3 weeks ago (Sept. 6, 2024, 7:52 p.m.) |
Issued | 22 years, 5 months ago (March 21, 2003) |
Published | 22 years, 5 months ago (March 21, 2003) |
Published Online | 22 years, 5 months ago (March 21, 2003) |
Published Print | 22 years, 4 months ago (April 1, 2003) |
@article{da_Fonseca_2003, title={Domain organization of the type 1 inositol 1,4,5-trisphosphate receptor as revealed by single-particle analysis}, volume={100}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.0536251100}, DOI={10.1073/pnas.0536251100}, number={7}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={da Fonseca, Paula C. A. and Morris, Stephen A. and Nerou, Edmund P. and Taylor, Colin W. and Morris, Edward P.}, year={2003}, month=mar, pages={3936–3941} }