Structural Biology of the Toll-Like Receptor Family

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dc.contributor.authorKang, Jin-Youngko
dc.contributor.authorLee, Jie-Ohko
dc.date.accessioned2013-03-09T11:27:12Z-
dc.date.available2013-03-09T11:27:12Z-
dc.date.created2012-02-06-
dc.date.created2012-02-06-
dc.date.created2012-02-06-
dc.date.issued2011-06-
dc.identifier.citationANNUAL REVIEW OF BIOCHEMISTRY, v.80, pp.917 - 941-
dc.identifier.issn0066-4154-
dc.identifier.urihttp://hdl.handle.net/10203/96228-
dc.description.abstractInnate immune receptors respond to common structural patterns in microbial molecules and are called pattern recognition receptors. Toll-like receptors (TLRs) play critical roles in the innate immune system by recognizing microbial lipids, carbohydrates, nucleic acids, and proteins. Precise definition of the ligand "pattern" of TLRs has been difficult to determine primarily owing to a lack of high-resolution structures. Recently, the structures of several TLR-ligand complexes and the intracellular signaling domains have been determined by X-ray crystallography. This new structural information, combined with extensive biochemical and immunological data accumulated over decades, sheds new light on ligand-recognition and -activation mechanisms. In this review, we summarize the TLR structures and discuss proposed ligand-recognition and -activation mechanisms.-
dc.languageEnglish-
dc.publisherANNUAL REVIEWS-
dc.titleStructural Biology of the Toll-Like Receptor Family-
dc.typeArticle-
dc.identifier.wosid000292895600036-
dc.identifier.scopusid2-s2.0-79959447465-
dc.type.rimsART-
dc.citation.volume80-
dc.citation.beginningpage917-
dc.citation.endingpage941-
dc.citation.publicationnameANNUAL REVIEW OF BIOCHEMISTRY-
dc.identifier.doi10.1146/annurev-biochem-052909-141507-
dc.embargo.liftdate9999-12-31-
dc.embargo.terms9999-12-31-
dc.contributor.localauthorKang, Jin-Young-
dc.contributor.localauthorLee, Jie-Oh-
dc.description.isOpenAccessN-
dc.type.journalArticleReview; Book Chapter-
dc.subject.keywordAuthorinnate immunity-
dc.subject.keywordAuthorpattern recognition-
dc.subject.keywordAuthorTLR-
dc.subject.keywordAuthorlipopolysaccharide-
dc.subject.keywordAuthorlipoprotein-
dc.subject.keywordAuthorinnate immunity-
dc.subject.keywordAuthorpattern recognition-
dc.subject.keywordAuthorTLR-
dc.subject.keywordAuthorlipopolysaccharide-
dc.subject.keywordAuthorlipoprotein-
dc.subject.keywordPlusMONOPHOSPHORYL-LIPID-A-
dc.subject.keywordPlusLEUCINE-RICH-REPEAT-
dc.subject.keywordPlusPEPTIDOGLYCAN-ASSOCIATED LIPOPROTEIN-
dc.subject.keywordPlusBORRELIA-BURGDORFERI LIPOPROTEINS-
dc.subject.keywordPlusDOUBLE-STRANDED-RNA-
dc.subject.keywordPlusCRYSTAL-STRUCTURE-
dc.subject.keywordPlusESCHERICHIA-COLI-
dc.subject.keywordPlusTIR-DOMAIN-
dc.subject.keywordPlusLIPOPOLYSACCHARIDE RECOGNITION-
dc.subject.keywordPlusBACTERIAL LIPOPOLYSACCHARIDE-
dc.subject.keywordPlusMONOPHOSPHORYL-LIPID-A-
dc.subject.keywordPlusLEUCINE-RICH-REPEAT-
dc.subject.keywordPlusPEPTIDOGLYCAN-ASSOCIATED LIPOPROTEIN-
dc.subject.keywordPlusBORRELIA-BURGDORFERI LIPOPROTEINS-
dc.subject.keywordPlusDOUBLE-STRANDED-RNA-
dc.subject.keywordPlusCRYSTAL-STRUCTURE-
dc.subject.keywordPlusESCHERICHIA-COLI-
dc.subject.keywordPlusTIR-DOMAIN-
dc.subject.keywordPlusLIPOPOLYSACCHARIDE RECOGNITION-
dc.subject.keywordPlusBACTERIAL LIPOPOLYSACCHARIDE-
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