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pubmed-article:20017190pubmed:abstractTextThe endoplasmic reticulum (ER) protein tapasin is essential for the loading of high-affinity peptides onto MHC class I molecules. It mediates peptide editing, i.e. the binding of peptides of successively higher affinity until class I molecules pass ER quality control and exit to the cell surface. The molecular mechanism of action of tapasin is unknown. We describe here the reconstitution of tapasin-mediated peptide editing on class I molecules in the lumen of microsomal membranes. We find that in a competitive situation between high- and low-affinity peptides, tapasin mediates the binding of the high-affinity peptide to class I by accelerating the dissociation of the peptide from an unstable intermediate of the binding reaction.lld:pubmed
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pubmed-article:20017190pubmed:authorpubmed-author:KalbacherHube...lld:pubmed
pubmed-article:20017190pubmed:authorpubmed-author:PraveenP V...lld:pubmed
pubmed-article:20017190pubmed:authorpubmed-author:SpringerSebas...lld:pubmed
pubmed-article:20017190pubmed:authorpubmed-author:YanevaRakinaRlld:pubmed
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pubmed-article:20017190pubmed:volume40lld:pubmed
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pubmed-article:20017190pubmed:pagination214-24lld:pubmed
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pubmed-article:20017190pubmed:year2010lld:pubmed
pubmed-article:20017190pubmed:articleTitleTapasin edits peptides on MHC class I molecules by accelerating peptide exchange.lld:pubmed
pubmed-article:20017190pubmed:affiliationBiochemistry and Cell Biology, Jacobs University Bremen, Bremen, Germany.lld:pubmed
pubmed-article:20017190pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:20017190pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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