Structure and function of Toll/interleukin-1 receptor/resistance protein (TIR) domains.

Ve, Thomas, Williams, Simon J. and Kobe, Bostjan (2014) Structure and function of Toll/interleukin-1 receptor/resistance protein (TIR) domains.. Apoptosis, 20 2: 250-261. doi:10.1007/s10495-014-1064-2

Author Ve, Thomas
Williams, Simon J.
Kobe, Bostjan
Title Structure and function of Toll/interleukin-1 receptor/resistance protein (TIR) domains.
Journal name Apoptosis   Check publisher's open access policy
ISSN 1360-8185
Publication date 2014-12-01
Year available 2014
Sub-type Article (original research)
DOI 10.1007/s10495-014-1064-2
Open Access Status
Volume 20
Issue 2
Start page 250
End page 261
Total pages 12
Place of publication New York, NY United States
Publisher Springer New York LLC
Language eng
Abstract The Toll/interleukin-1 receptor/resistance protein (TIR) domain is a protein-protein interaction domain consisting of 125-200 residues, widely distributed in animals, plants and bacteria but absent from fungi, archea and viruses. In plants and animals, these domains are found in proteins with functions in innate immune pathways, while in bacteria, some TIR domain-containing proteins interfere with the innate immune pathways in the host. TIR domains function as protein scaffolds, mostly involving self-association and homotypic interactions with other TIR domains. In the last 15 years, the three-dimensional structures of TIR domains from several mammalian, plant and bacterial proteins have been reported. These structures, jointly with functional data including the identification of interacting proteins, have started to provide insight into the molecular basis of the assembly of animal and plant immune signaling complexes, and for host immunosuppression by bacterial pathogens. This review focuses on the current knowledge of the structures of the TIR domains and how the structure relates to function.
Keyword Biochemistry & Molecular Biology
Cell Biology
Biochemistry & Molecular Biology
Cell Biology
Q-Index Code C1
Q-Index Status Confirmed Code
Grant ID 1003326
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2015 Collection
School of Chemistry and Molecular Biosciences
Institute for Molecular Bioscience - Publications
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Citation counts: TR Web of Science Citation Count  Cited 34 times in Thomson Reuters Web of Science Article | Citations
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Created: Fri, 05 Dec 2014, 20:40:31 EST by Mrs Louise Nimwegen on behalf of School of Chemistry & Molecular Biosciences