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http://purl.uniprot.org/citations/21857663http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21857663http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21857663http://www.w3.org/2000/01/rdf-schema#comment"RP105-MD-1 modulates the TLR4-MD-2-mediated, innate immune response against bacterial lipopolysaccharide (LPS). The crystal structure of the bovine 1:1 RP105-MD-1 complex bound to a putative endogenous lipid at 2.9 Å resolution shares a similar overall architecture to its homolog TLR4-MD-2 but assembles into an unusual 2:2 homodimer that differs from any other known TLR-ligand assembly. The homodimer is assembled in a head-to-head orientation that juxtaposes the N-terminal leucine-rich repeats (LRRs) of the two RP105 chains, rather than the usual tail-to-tail configuration of C-terminal LRRs in ligand-activated TLR dimers, such as TLR1-TRL2, TLR2-TLR6, TLR3-TLR3 and TLR4-TLR4. Another unusual interaction is mediated by an RP105-specific asparagine-linked glycan, which wedges MD-1 into the co-receptor binding concavity on RP105. This unique mode of assembly represents a new paradigm for TLR complexes and suggests a molecular mechanism for regulating LPS responses."xsd:string
http://purl.uniprot.org/citations/21857663http://purl.org/dc/terms/identifier"doi:10.1038/nsmb.2106"xsd:string
http://purl.uniprot.org/citations/21857663http://purl.org/dc/terms/identifier"doi:10.1038/nsmb.2106"xsd:string
http://purl.uniprot.org/citations/21857663http://purl.uniprot.org/core/author"Wilson I.A."xsd:string
http://purl.uniprot.org/citations/21857663http://purl.uniprot.org/core/author"Wilson I.A."xsd:string
http://purl.uniprot.org/citations/21857663http://purl.uniprot.org/core/author"Hong M."xsd:string
http://purl.uniprot.org/citations/21857663http://purl.uniprot.org/core/author"Hong M."xsd:string
http://purl.uniprot.org/citations/21857663http://purl.uniprot.org/core/author"Yoon S.I."xsd:string
http://purl.uniprot.org/citations/21857663http://purl.uniprot.org/core/author"Yoon S.I."xsd:string
http://purl.uniprot.org/citations/21857663http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21857663http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21857663http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/21857663http://purl.uniprot.org/core/name"Nat Struct Mol Biol"xsd:string
http://purl.uniprot.org/citations/21857663http://purl.uniprot.org/core/pages"1028-1035"xsd:string
http://purl.uniprot.org/citations/21857663http://purl.uniprot.org/core/pages"1028-1035"xsd:string
http://purl.uniprot.org/citations/21857663http://purl.uniprot.org/core/title"An unusual dimeric structure and assembly for TLR4 regulator RP105-MD-1."xsd:string
http://purl.uniprot.org/citations/21857663http://purl.uniprot.org/core/title"An unusual dimeric structure and assembly for TLR4 regulator RP105-MD-1."xsd:string
http://purl.uniprot.org/citations/21857663http://purl.uniprot.org/core/volume"18"xsd:string
http://purl.uniprot.org/citations/21857663http://purl.uniprot.org/core/volume"18"xsd:string
http://purl.uniprot.org/citations/21857663http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21857663
http://purl.uniprot.org/citations/21857663http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21857663
http://purl.uniprot.org/citations/21857663http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21857663
http://purl.uniprot.org/citations/21857663http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21857663