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http://purl.uniprot.org/citations/24065820http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24065820http://www.w3.org/2000/01/rdf-schema#comment"Complement receptors (CRs), expressed notably on myeloid and lymphoid cells, play an essential function in the elimination of complement-opsonized pathogens and apoptotic/necrotic cells. In addition, these receptors are crucial for the cross-talk between the innate and adaptive branches of the immune system. CR3 (also known as Mac-1, integrin αMβ2, or CD11b/CD18) is expressed on all macrophages and recognizes iC3b on complement-opsonized objects, enabling their phagocytosis. We demonstrate that the C3d moiety of iC3b harbors the binding site for the CR3 αI domain, and our structure of the C3d:αI domain complex rationalizes the CR3 selectivity for iC3b. Based on extensive structural analysis, we suggest that the choice between a ligand glutamate or aspartate for coordination of a receptor metal ion-dependent adhesion site-bound metal ion is governed by the secondary structure of the ligand. Comparison of our structure to the CR2:C3d complex and the in vitro formation of a stable CR3:C3d:CR2 complex suggests a molecular mechanism for the hand-over of CR3-bound immune complexes from macrophages to CR2-presenting cells in lymph nodes."xsd:string
http://purl.uniprot.org/citations/24065820http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1311261110"xsd:string
http://purl.uniprot.org/citations/24065820http://purl.uniprot.org/core/author"Yatime L."xsd:string
http://purl.uniprot.org/citations/24065820http://purl.uniprot.org/core/author"Sim R.B."xsd:string
http://purl.uniprot.org/citations/24065820http://purl.uniprot.org/core/author"Vorup-Jensen T."xsd:string
http://purl.uniprot.org/citations/24065820http://purl.uniprot.org/core/author"Andersen G.R."xsd:string
http://purl.uniprot.org/citations/24065820http://purl.uniprot.org/core/author"Bajic G."xsd:string
http://purl.uniprot.org/citations/24065820http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/24065820http://purl.uniprot.org/core/name"Proc Natl Acad Sci U S A"xsd:string
http://purl.uniprot.org/citations/24065820http://purl.uniprot.org/core/pages"16426-16431"xsd:string
http://purl.uniprot.org/citations/24065820http://purl.uniprot.org/core/title"Structural insight on the recognition of surface-bound opsonins by the integrin I domain of complement receptor 3."xsd:string
http://purl.uniprot.org/citations/24065820http://purl.uniprot.org/core/volume"110"xsd:string
http://purl.uniprot.org/citations/24065820http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24065820
http://purl.uniprot.org/citations/24065820http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24065820
http://purl.uniprot.org/uniprot/#_P11215-mappedCitation-24065820http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24065820
http://purl.uniprot.org/uniprot/#_P01024-mappedCitation-24065820http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24065820
http://purl.uniprot.org/uniprot/P11215http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/24065820
http://purl.uniprot.org/uniprot/P01024http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/24065820