| pubmed-article:10357804 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10357804 | lifeskim:mentions | umls-concept:C0025007 | lld:lifeskim |
| pubmed-article:10357804 | lifeskim:mentions | umls-concept:C0285488 | lld:lifeskim |
| pubmed-article:10357804 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:10357804 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:10357804 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:10357804 | lifeskim:mentions | umls-concept:C0205148 | lld:lifeskim |
| pubmed-article:10357804 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:10357804 | lifeskim:mentions | umls-concept:C0231449 | lld:lifeskim |
| pubmed-article:10357804 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:10357804 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:10357804 | pubmed:dateCreated | 1999-8-5 | lld:pubmed |
| pubmed-article:10357804 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10357804 | pubmed:abstractText | Measles virus is a paramyxovirus which, like other members of the family such as respiratory syncytial virus, is a major cause of morbidity and mortality worldwide. The cell surface receptor for measles virus in humans is CD46, a complement cofactor. We report here the crystal structure at 3.1 A resolution of the measles virus-binding fragment of CD46. The structure reveals the architecture and spatial arrangement of two glycosylated short consensus repeats with a pronounced interdomain bend and some flexibility at the domain interface. Amino acids involved in measles virus binding define a large, glycan-free surface that extends from the top of the first to the bottom of the second repeat. The extended virus-binding surface of CD46 differs strikingly from those reported for the human virus receptor proteins CD4 and intercellular cell adhesion molecule-1 (ICAM-1), suggesting that the CD46 structure utilizes a novel mode of virus recognition. A highly hydrophobic and protruding loop at the base of the first repeat bears a critical virus-binding residue, thereby defining an important recognition epitope. Molecules that mimic the conformation of this loop potentially could be effective anti-viral agents by preventing binding of measles virus to CD46. | lld:pubmed |
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| pubmed-article:10357804 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10357804 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10357804 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10357804 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10357804 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10357804 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10357804 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10357804 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:10357804 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:10357804 | pubmed:author | pubmed-author:StehleTT | lld:pubmed |
| pubmed-article:10357804 | pubmed:author | pubmed-author:CasasnovasJ... | lld:pubmed |
| pubmed-article:10357804 | pubmed:author | pubmed-author:LarvieMM | lld:pubmed |
| pubmed-article:10357804 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10357804 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:10357804 | pubmed:volume | 18 | lld:pubmed |
| pubmed-article:10357804 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10357804 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10357804 | pubmed:pagination | 2911-22 | lld:pubmed |
| pubmed-article:10357804 | pubmed:dateRevised | 2010-9-10 | lld:pubmed |
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