pubmed-article:10318936 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10318936 | lifeskim:mentions | umls-concept:C0019629 | lld:lifeskim |
pubmed-article:10318936 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
pubmed-article:10318936 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:10318936 | lifeskim:mentions | umls-concept:C0591833 | lld:lifeskim |
pubmed-article:10318936 | pubmed:issue | 10 | lld:pubmed |
pubmed-article:10318936 | pubmed:dateCreated | 1999-6-17 | lld:pubmed |
pubmed-article:10318936 | pubmed:abstractText | MHC molecules are expressed at the surface of nucleated cells to present peptides to T cells. Structural information on MHC molecules has been gathered by x-ray crystallography techniques by using soluble proteins. Although relationships between MHC molecules and cell membranes have not been studied in detail, they are of critical importance for T cell recognition. Using a chemically modified lipid, we have been able to capture and orient histidine-tagged MHC molecules on lipid membranes. Surface plasmon resonance experiments show that the protein binds to the nickel lipid in a specific manner and in an oriented fashion, which allows T cell receptor binding. Similar lipid surfaces have been used to grow two-dimensional crystals and to determine the structure of a membrane-anchored murine H-2Kb MHC class I molecule. The docking of the crystallographic structure into the three-dimensional reconstructed structure derived from the two-dimensional crystals allows us to determine that the histidine tag is near the membrane surface and that the MHC molecule is in an upright position, exposing the peptide/alpha1-alpha2 domains toward the T cell. | lld:pubmed |
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pubmed-article:10318936 | pubmed:language | eng | lld:pubmed |
pubmed-article:10318936 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10318936 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10318936 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10318936 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10318936 | pubmed:month | May | lld:pubmed |
pubmed-article:10318936 | pubmed:issn | 0027-8424 | lld:pubmed |
pubmed-article:10318936 | pubmed:author | pubmed-author:MilliganR ARA | lld:pubmed |
pubmed-article:10318936 | pubmed:author | pubmed-author:TeytonLL | lld:pubmed |
pubmed-article:10318936 | pubmed:author | pubmed-author:CelikFF | lld:pubmed |
pubmed-article:10318936 | pubmed:author | pubmed-author:Wilson-Kubale... | lld:pubmed |
pubmed-article:10318936 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10318936 | pubmed:day | 11 | lld:pubmed |
pubmed-article:10318936 | pubmed:volume | 96 | lld:pubmed |
pubmed-article:10318936 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10318936 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10318936 | pubmed:pagination | 5634-9 | lld:pubmed |
pubmed-article:10318936 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:10318936 | pubmed:meshHeading | pubmed-meshheading:10318936... | lld:pubmed |
pubmed-article:10318936 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10318936 | pubmed:articleTitle | Structure and function of a membrane-bound murine MHC class I molecule. | lld:pubmed |
pubmed-article:10318936 | pubmed:affiliation | Department of Immunology, The Scripps Research Institute, 10550, North Torrey Pines Road, La Jolla, CA 92037, USA. | lld:pubmed |
pubmed-article:10318936 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10318936 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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