| pubmed-article:17901336 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17901336 | lifeskim:mentions | umls-concept:C0003241 | lld:lifeskim |
| pubmed-article:17901336 | lifeskim:mentions | umls-concept:C1332700 | lld:lifeskim |
| pubmed-article:17901336 | lifeskim:mentions | umls-concept:C1332714 | lld:lifeskim |
| pubmed-article:17901336 | lifeskim:mentions | umls-concept:C1291802 | lld:lifeskim |
| pubmed-article:17901336 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:17901336 | pubmed:issue | 5846 | lld:pubmed |
| pubmed-article:17901336 | pubmed:dateCreated | 2007-9-28 | lld:pubmed |
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| pubmed-article:17901336 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17901336 | pubmed:abstractText | 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. | lld:pubmed |
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| pubmed-article:17901336 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17901336 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17901336 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17901336 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17901336 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:17901336 | pubmed:issn | 1095-9203 | lld:pubmed |
| pubmed-article:17901336 | pubmed:author | pubmed-author:WilsonIan AIA | lld:pubmed |
| pubmed-article:17901336 | pubmed:author | pubmed-author:RobinsonJames... | lld:pubmed |
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| pubmed-article:17901336 | pubmed:author | pubmed-author:WyattRichardR | lld:pubmed |
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| pubmed-article:17901336 | pubmed:author | pubmed-author:LamSon NSN | lld:pubmed |
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| pubmed-article:17901336 | pubmed:author | pubmed-author:TangMinM | lld:pubmed |
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| pubmed-article:17901336 | pubmed:author | pubmed-author:HuangChih-Chi... | lld:pubmed |
| pubmed-article:17901336 | pubmed:author | pubmed-author:HussanSyed... | lld:pubmed |
| pubmed-article:17901336 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17901336 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:17901336 | pubmed:volume | 317 | lld:pubmed |
| pubmed-article:17901336 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17901336 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17901336 | pubmed:pagination | 1930-4 | lld:pubmed |
| pubmed-article:17901336 | pubmed:dateRevised | 2011-9-19 | lld:pubmed |
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| pubmed-article:17901336 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17901336 | pubmed:articleTitle | Structures of the CCR5 N terminus and of a tyrosine-sulfated antibody with HIV-1 gp120 and CD4. | lld:pubmed |
| pubmed-article:17901336 | pubmed:affiliation | Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA. | lld:pubmed |
| pubmed-article:17901336 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17901336 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:17901336 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:17901336 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| pubmed-article:17901336 | pubmed:publicationType | Research Support, N.I.H., Intramural | lld:pubmed |
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