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pubmed-article:10318936pubmed:abstractTextMHC 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:10318936pubmed:articleTitleStructure and function of a membrane-bound murine MHC class I molecule.lld:pubmed
pubmed-article:10318936pubmed:affiliationDepartment of Immunology, The Scripps Research Institute, 10550, North Torrey Pines Road, La Jolla, CA 92037, USA.lld:pubmed
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pubmed-article:10318936pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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