pubmed-article:10748229 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10748229 | lifeskim:mentions | umls-concept:C0007004 | lld:lifeskim |
pubmed-article:10748229 | lifeskim:mentions | umls-concept:C1523873 | lld:lifeskim |
pubmed-article:10748229 | lifeskim:mentions | umls-concept:C0065684 | lld:lifeskim |
pubmed-article:10748229 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
pubmed-article:10748229 | lifeskim:mentions | umls-concept:C1511603 | lld:lifeskim |
pubmed-article:10748229 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
pubmed-article:10748229 | pubmed:issue | 7 | lld:pubmed |
pubmed-article:10748229 | pubmed:dateCreated | 2000-6-8 | lld:pubmed |
pubmed-article:10748229 | pubmed:abstractText | The macrophage and epithelial cell mannose receptor (MR) binds carbohydrates on foreign and host molecules. Two portions of MR recognize carbohydrates: tandemly arranged C-type lectin domains facilitate carbohydrate-dependent macrophage uptake of infectious organisms, and the NH(2)-terminal cysteine-rich domain (Cys-MR) binds to sulfated glycoproteins including pituitary hormones. To elucidate the mechanism of sulfated carbohydrate recognition, we determined crystal structures of Cys-MR alone and complexed with 4-sulfated-N-acetylgalactosamine at 1.7 and 2.2 A resolution, respectively. Cys-MR folds into an approximately three-fold symmetric beta-trefoil shape resembling fibroblast growth factor. The sulfate portions of 4-sulfated-N-acetylgalactosamine and an unidentified ligand found in the native crystals bind in a neutral pocket in the third lobe. We use the structures to rationalize the carbohydrate binding specificities of Cys-MR and compare the recognition properties of Cys-MR with other beta-trefoil proteins. | lld:pubmed |
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pubmed-article:10748229 | pubmed:language | eng | lld:pubmed |
pubmed-article:10748229 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10748229 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10748229 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10748229 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10748229 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10748229 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10748229 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10748229 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10748229 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10748229 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10748229 | pubmed:month | Apr | lld:pubmed |
pubmed-article:10748229 | pubmed:issn | 0022-1007 | lld:pubmed |
pubmed-article:10748229 | pubmed:author | pubmed-author:FeiziTT | lld:pubmed |
pubmed-article:10748229 | pubmed:author | pubmed-author:BjorkmanP JPJ | lld:pubmed |
pubmed-article:10748229 | pubmed:author | pubmed-author:LieII | lld:pubmed |
pubmed-article:10748229 | pubmed:author | pubmed-author:MisulovinZZ | lld:pubmed |
pubmed-article:10748229 | pubmed:author | pubmed-author:NussenzweigM... | lld:pubmed |
pubmed-article:10748229 | pubmed:author | pubmed-author:ChirinoA JAJ | lld:pubmed |
pubmed-article:10748229 | pubmed:author | pubmed-author:LeteuxCC | lld:pubmed |
pubmed-article:10748229 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10748229 | pubmed:day | 3 | lld:pubmed |
pubmed-article:10748229 | pubmed:volume | 191 | lld:pubmed |
pubmed-article:10748229 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10748229 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10748229 | pubmed:pagination | 1105-16 | lld:pubmed |
pubmed-article:10748229 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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