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dc.contributor.authorNimma, Surekha
dc.contributor.authorVe, Thomas
dc.contributor.authorWilliams, Simon J
dc.contributor.authorKobe, Bostjan
dc.date.accessioned2017-08-10T01:18:52Z
dc.date.available2017-08-10T01:18:52Z
dc.date.issued2017
dc.identifier.issn0959-440X
dc.identifier.doi10.1016/j.sbi.2016.12.014
dc.identifier.urihttp://hdl.handle.net/10072/343700
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.peerreviewedYes
dc.languageEnglish
dc.publisherElsevier
dc.relation.ispartofpagefrom122
dc.relation.ispartofpageto130
dc.relation.ispartofjournalCurrent Opinion in Structural Biology
dc.relation.ispartofvolume43
dc.subject.fieldofresearchBiochemistry and Cell Biology not elsewhere classified
dc.subject.fieldofresearchMedicinal and Biomolecular Chemistry
dc.subject.fieldofresearchBiochemistry and Cell Biology
dc.subject.fieldofresearchcode060199
dc.subject.fieldofresearchcode0304
dc.subject.fieldofresearchcode0601
dc.titleTowards the structure of the TIR-domain signalosome
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.hasfulltextNo Full Text
gro.griffith.authorVe, Thomas


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