The University of Dublin | Trinity College -- Ollscoil Átha Cliath | Coláiste na Tríonóide
Trinity's Access to Research Archive
Home :: Log In :: Submit :: Alerts ::

School of Biochemistry & Immunology >
Biochemistry >
Biochemistry (Scholarly Publications) >

Please use this identifier to cite or link to this item:

Title: Crystal structure of the Toll/interleukin-1 receptor domain of human IL-1RAPL
Sponsor: National Institutes of Health (NIH)
Author's Homepage:
Keywords: Biochemistry
Issue Date: 2004
Publisher: The American Society for Biochemistry and Molecular Biology
Citation: Khan JA, Brint EK, O'Neill LAJ, Tong L ‘Crystal structure of the Toll/interleukin-1 receptor domain of human IL-1RAPL’ in Journal of Biological Chemistry, 279, (30), 2004, pp 31664 - 31670
Series/Report no.: Journal of Biological Chemistry
Abstract: The Toll/interleukin-1 receptor (TIR) domain is conserved in the intracellular regions of Toll-like receptors (TLRs) and interleukin-1 receptors (IL-1Rs) as well as in several cytoplasmic adapter molecules. This domain has crucial roles in signal transduction by these receptors for host immune response. Here we report the crystal structure at 2.3-Å resolution of the TIR domain of human IL-1RAPL, the first structure of a TIR domain of the IL-1R superfamily. There are large structural differences between this TIR domain and that of TLR1 and TLR2. Helix αD in IL-1RAPL is almost perpendicular to its equivalent in TLR1 or TLR2. The BB loop contains a hydrogen bond unique to IL-1RAPL between Thr residues at the 8th and 10th positions. The structural and sequence diversity among these domains may be important for specificity in the signal transduction by these receptors. A dimer of the TIR domain of IL-1RAPL is observed in the crystal, although this domain is monomeric in solution. Residues in the dimer interface are mostly unique to IL-1RAPL, which is consistent with the distinct functional roles of this receptor. Our functional studies show IL-1RAPL can activate JNK but not the ERK or the p38 MAP kinases, whereas its close homolog, TIGIRR, cannot activate JNK. Deletion mutagenesis studies show that the activation of JNK by IL-1RAPL does not depend on the integrity of its TIR domain, suggesting a distinct mechanism of signaling through this receptor.
Description: PUBLISHED
Appears in Collections:Biochemistry (Scholarly Publications)

Files in This Item:

File Description SizeFormat
Crystal structure of the Toll interleukin-1 receptor domain of human IL-1RAPL.pdfpublished (publisher copy) peer-reviewed788.94 kBAdobe PDFView/Open

This item is protected by original copyright

Please note: There is a known bug in some browsers that causes an error when a user tries to view large pdf file within the browser window. If you receive the message "The file is damaged and could not be repaired", please try one of the solutions linked below based on the browser you are using.

Items in TARA are protected by copyright, with all rights reserved, unless otherwise indicated.


Valid XHTML 1.0! DSpace Software Copyright © 2002-2010  Duraspace - Feedback