| pubmed-article:11864610 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:11864610 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:11864610 | lifeskim:mentions | umls-concept:C0019768 | lld:lifeskim |
| pubmed-article:11864610 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:11864610 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:11864610 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:11864610 | lifeskim:mentions | umls-concept:C2825311 | lld:lifeskim |
| pubmed-article:11864610 | lifeskim:mentions | umls-concept:C2349209 | lld:lifeskim |
| pubmed-article:11864610 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:11864610 | pubmed:dateCreated | 2002-2-26 | lld:pubmed |
| pubmed-article:11864610 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11864610 | pubmed:abstractText | Epstein-Barr virus (EBV) causes infectious mononucleosis, establishes long-term latent infections, and is associated with a variety of human tumors. The EBV gp42 glycoprotein binds MHC class II molecules, playing a critical role in infection of B lymphocytes. EBV gp42 belongs to the C-type lectin superfamily, with homology to NK receptors of the immune system. We report the crystal structure of gp42 bound to the human MHC class II molecule HLA-DR1. The gp42 binds HLA-DR1 using a surface site that is distinct from the canonical lectin and NK receptor ligand binding sites. At the canonical ligand binding site, gp42 forms a large hydrophobic groove, which could interact with other ligands necessary for EBV entry, providing a mechanism for coupling MHC recognition and membrane fusion. | lld:pubmed |
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| pubmed-article:11864610 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11864610 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11864610 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11864610 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11864610 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:11864610 | pubmed:issn | 1097-2765 | lld:pubmed |
| pubmed-article:11864610 | pubmed:author | pubmed-author:LongneckerRic... | lld:pubmed |
| pubmed-article:11864610 | pubmed:author | pubmed-author:MullenMaureen... | lld:pubmed |
| pubmed-article:11864610 | pubmed:author | pubmed-author:HaanKeith MKM | lld:pubmed |
| pubmed-article:11864610 | pubmed:author | pubmed-author:JardetzkyTheo... | lld:pubmed |
| pubmed-article:11864610 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11864610 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:11864610 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11864610 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11864610 | pubmed:pagination | 375-85 | lld:pubmed |
| pubmed-article:11864610 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:11864610 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11864610 | pubmed:articleTitle | Structure of the Epstein-Barr virus gp42 protein bound to the MHC class II receptor HLA-DR1. | lld:pubmed |
| pubmed-article:11864610 | pubmed:affiliation | Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208, USA. | lld:pubmed |
| pubmed-article:11864610 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11864610 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:11864610 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11864610 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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