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http://purl.uniprot.org/citations/17901336http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17901336http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17901336http://www.w3.org/2000/01/rdf-schema#comment"The CCR5 co-receptor binds to the HIV-1 gp120 envelope glycoprotein and facilitates HIV-1 entry into cells. Its N terminus is tyrosine-sulfated, as are many antibodies that react with the co-receptor binding site on gp120. We applied nuclear magnetic resonance and crystallographic techniques to analyze the structure of the CCR5 N terminus and that of the tyrosine-sulfated antibody 412d in complex with gp120 and CD4. The conformations of tyrosine-sulfated regions of CCR5 (alpha-helix) and 412d (extended loop) are surprisingly different. Nonetheless, a critical sulfotyrosine on CCR5 and on 412d induces similar structural rearrangements in gp120. These results now provide a framework for understanding HIV-1 interactions with the CCR5 N terminus during viral entry and define a conserved site on gp120, whose recognition of sulfotyrosine engenders posttranslational mimicry by the immune system."xsd:string
http://purl.uniprot.org/citations/17901336http://purl.org/dc/terms/identifier"doi:10.1126/science.1145373"xsd:string
http://purl.uniprot.org/citations/17901336http://purl.org/dc/terms/identifier"doi:10.1126/science.1145373"xsd:string
http://purl.uniprot.org/citations/17901336http://purl.uniprot.org/core/author"Huang C.C."xsd:string
http://purl.uniprot.org/citations/17901336http://purl.uniprot.org/core/author"Huang C.C."xsd:string
http://purl.uniprot.org/citations/17901336http://purl.uniprot.org/core/author"Wilson I.A."xsd:string
http://purl.uniprot.org/citations/17901336http://purl.uniprot.org/core/author"Wilson I.A."xsd:string
http://purl.uniprot.org/citations/17901336http://purl.uniprot.org/core/author"Tang M."xsd:string
http://purl.uniprot.org/citations/17901336http://purl.uniprot.org/core/author"Tang M."xsd:string
http://purl.uniprot.org/citations/17901336http://purl.uniprot.org/core/author"Robinson J."xsd:string
http://purl.uniprot.org/citations/17901336http://purl.uniprot.org/core/author"Robinson J."xsd:string
http://purl.uniprot.org/citations/17901336http://purl.uniprot.org/core/author"Kwong P.D."xsd:string
http://purl.uniprot.org/citations/17901336http://purl.uniprot.org/core/author"Kwong P.D."xsd:string
http://purl.uniprot.org/citations/17901336http://purl.uniprot.org/core/author"Sodroski J."xsd:string
http://purl.uniprot.org/citations/17901336http://purl.uniprot.org/core/author"Sodroski J."xsd:string
http://purl.uniprot.org/citations/17901336http://purl.uniprot.org/core/author"Stanfield R.L."xsd:string
http://purl.uniprot.org/citations/17901336http://purl.uniprot.org/core/author"Stanfield R.L."xsd:string
http://purl.uniprot.org/citations/17901336http://purl.uniprot.org/core/author"Wyatt R."xsd:string
http://purl.uniprot.org/citations/17901336http://purl.uniprot.org/core/author"Wyatt R."xsd:string
http://purl.uniprot.org/citations/17901336http://purl.uniprot.org/core/author"Xiang S.H."xsd:string
http://purl.uniprot.org/citations/17901336http://purl.uniprot.org/core/author"Xiang S.H."xsd:string
http://purl.uniprot.org/citations/17901336http://purl.uniprot.org/core/author"Acharya P."xsd:string
http://purl.uniprot.org/citations/17901336http://purl.uniprot.org/core/author"Acharya P."xsd:string