NDLI: Domain organization of the type 1 inositol 1,4,5-trisphosphate receptor as revealed by single-particle analysis.

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Domain organization of the type 1 inositol 1,4,5-trisphosphate receptor as revealed by single-particle analysis.

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Domain organization of the type 1 inositol 1,4,5-trisphosphate receptor as revealed by single-particle analysis.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Morris, Stephen A. Nerou, Edmund P. Da Fonseca, Paula C. A. Morris, Edward P. Taylor, Colin W.
Description	Author Affiliation: da Fonseca PC ( Biomedical Sciences Division, Sir Alexander Fleming Building, Imperial College of Science Technology and Medicine, London SW7 2AZ, United Kingdom.);
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.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	7
Volume Number	100
Language	English
Publisher	National Academy of Sciences
Publisher Date	2003-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Calcium Channels Chemistry Ultrastructure Receptors, Cytoplasmic And Nuclear Animals Isolation & Purification Cell Membrane Cerebellum Cytoplasm Image Processing, Computer-Assisted Inositol 1,4,5-Trisphosphate Receptors Ion Channels Microscopy, Electron Protein Conformation Protein Structure, Secondary Protein Subunits Comparative Study Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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