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http://purl.uniprot.org/citations/23453971http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23453971http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23453971http://www.w3.org/2000/01/rdf-schema#comment"Tank-binding kinase I (TBK1) plays a key role in the innate immune system by integrating signals from pattern-recognition receptors. Here, we report the X-ray crystal structures of inhibitor-bound inactive and active TBK1 determined to 2.6 Å and 4.0 Å resolution, respectively. The structures reveal a compact dimer made up of trimodular subunits containing an N-terminal kinase domain (KD), a ubiquitin-like domain (ULD), and an α-helical scaffold dimerization domain (SDD). Activation rearranges the KD into an active conformation while maintaining the overall dimer conformation. Low-resolution SAXS studies reveal that the missing C-terminal domain (CTD) extends away from the main body of the kinase dimer. Mutants that interfere with TBK1 dimerization show significantly reduced trans-autophosphorylation but retain the ability to bind adaptor proteins through the CTD. Our results provide detailed insights into the architecture of TBK1 and the molecular mechanism of activation."xsd:string
http://purl.uniprot.org/citations/23453971http://purl.org/dc/terms/identifier"doi:10.1016/j.celrep.2013.01.034"xsd:string
http://purl.uniprot.org/citations/23453971http://purl.org/dc/terms/identifier"doi:10.1016/j.celrep.2013.01.034"xsd:string
http://purl.uniprot.org/citations/23453971http://purl.uniprot.org/core/author"Devos J.M."xsd:string
http://purl.uniprot.org/citations/23453971http://purl.uniprot.org/core/author"Devos J.M."xsd:string
http://purl.uniprot.org/citations/23453971http://purl.uniprot.org/core/author"Round A."xsd:string
http://purl.uniprot.org/citations/23453971http://purl.uniprot.org/core/author"Round A."xsd:string
http://purl.uniprot.org/citations/23453971http://purl.uniprot.org/core/author"Nanao M.H."xsd:string
http://purl.uniprot.org/citations/23453971http://purl.uniprot.org/core/author"Nanao M.H."xsd:string
http://purl.uniprot.org/citations/23453971http://purl.uniprot.org/core/author"Maniatis T."xsd:string
http://purl.uniprot.org/citations/23453971http://purl.uniprot.org/core/author"Maniatis T."xsd:string
http://purl.uniprot.org/citations/23453971http://purl.uniprot.org/core/author"Panne D."xsd:string
http://purl.uniprot.org/citations/23453971http://purl.uniprot.org/core/author"Panne D."xsd:string
http://purl.uniprot.org/citations/23453971http://purl.uniprot.org/core/author"Ng S.L."xsd:string
http://purl.uniprot.org/citations/23453971http://purl.uniprot.org/core/author"Ng S.L."xsd:string
http://purl.uniprot.org/citations/23453971http://purl.uniprot.org/core/author"Larabi A."xsd:string
http://purl.uniprot.org/citations/23453971http://purl.uniprot.org/core/author"Larabi A."xsd:string
http://purl.uniprot.org/citations/23453971http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23453971http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23453971http://purl.uniprot.org/core/name"Cell Rep."xsd:string
http://purl.uniprot.org/citations/23453971http://purl.uniprot.org/core/name"Cell Rep."xsd:string
http://purl.uniprot.org/citations/23453971http://purl.uniprot.org/core/pages"734-746"xsd:string
http://purl.uniprot.org/citations/23453971http://purl.uniprot.org/core/pages"734-746"xsd:string