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Towards the structure of the TIR-domain signalosome

Nimma, Surekha; Ve, Thomas; Williams, Simon; Kobe, Bostjan

Description

TIR (Toll/interleukin-1 receptor/resistance protein) domains feature in animal, plant and bacterial proteins involved in innate immunity pathways and associated processes. They function through protein:protein interactions, in particular self-association and homotypic association with other TIR domains. Structures of TIR domains from all phyla have been determined, but common association modes have only emerged for plant and bacterial TIR domains, and not for mammalian TIR domains. Numerous...[Show more]

dc.contributor.authorNimma, Surekha
dc.contributor.authorVe, Thomas
dc.contributor.authorWilliams, Simon
dc.contributor.authorKobe, Bostjan
dc.date.accessioned2021-10-07T23:20:38Z
dc.identifier.issn0959-440X
dc.identifier.urihttp://hdl.handle.net/1885/250555
dc.description.abstractTIR (Toll/interleukin-1 receptor/resistance protein) domains feature in animal, plant and bacterial proteins involved in innate immunity pathways and associated processes. They function through protein:protein interactions, in particular self-association and homotypic association with other TIR domains. Structures of TIR domains from all phyla have been determined, but common association modes have only emerged for plant and bacterial TIR domains, and not for mammalian TIR domains. Numerous attempts involving hybrid approaches, which have combined structural, computational, mutagenesis and biophysical data, have failed to converge onto common models of how these domains associate and function. We propose that the available data can be reconciled in the context of higher-order assembly formation, and that TIR domains function through signaling by cooperative assembly formation (SCAF).
dc.description.sponsorshipThe work in the authors’ laboratories was supported by the National Health and Medical Research Council (NHMRC grants 1003326, 1107804, 1071659) and the Australian Research Council (ARC Discovery Projects DP120100685, DP160102244). BK is NHMRC Principal Research Fellow (1003325, 1110971). Simon Williams is funded by ARC DECRA (DE160100893). We acknowledge the use of the University of Queensland Remote Operation Crystallization and X-ray Diffraction Facility (UQ ROCX) and the Australian Synchrotron (MX and SAXSWAXS beamlines) for our structural work.
dc.format.mimetypeapplication/pdf
dc.language.isoen_AU
dc.publisherElsevier
dc.rights© 2017 Elsevier Ltd
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.sourceCurrent Opinion in Structural Biology
dc.titleTowards the structure of the TIR-domain signalosome
dc.typeJournal article
local.description.notesImported from ARIES
local.identifier.citationvolume43
dc.date.issued2017
local.identifier.absfor060112 - Structural Biology (incl. Macromolecular Modelling)
local.identifier.ariespublicationu4956746xPUB631
local.publisher.urlhttps://www.elsevier.com/en-au
local.type.statusAccepted Version
local.contributor.affiliationNimma, Surekha, University of Queensland
local.contributor.affiliationVe, Thomas , University of Queensland
local.contributor.affiliationWilliams, Simon, College of Science, ANU
local.contributor.affiliationKobe, Bostjan, University of Queensland
dc.relationhttp://purl.org/au-research/grants/arc/DP120100685
dc.relationhttp://purl.org/au-research/grants/arc/DP160102244
dc.relationhttp://purl.org/au-research/grants/arc/DE160100893
dc.relationhttp://purl.org/au-research/grants/nhmrc/1003326
dc.relationhttp://purl.org/au-research/grants/nhmrc/1107804
dc.relationhttp://purl.org/au-research/grants/nhmrc/1071659
local.bibliographicCitation.issue1
local.bibliographicCitation.startpage122
local.bibliographicCitation.lastpage130
local.identifier.doi10.1016/j.sbi.2016.12.014
local.identifier.absseo970106 - Expanding Knowledge in the Biological Sciences
dc.date.updated2020-11-23T11:23:21Z
local.identifier.scopusID2-s2.0-85009165959
local.identifier.thomsonID000403460500017
dcterms.accessRightsOpen Access
dc.provenancehttps://v2.sherpa.ac.uk/id/publication/11158..."The Accepted Version can be archived in an Institutional Repository. 12 Months. CC BY-NC-ND." from SHERPA/RoMEO site (as at 11/10/2021).
dc.rights.licenseCC BY-NC-ND
CollectionsANU Research Publications

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