Journal
EUROPEAN JOURNAL OF IMMUNOLOGY
Volume 40, Issue 1, Pages 214-224Publisher
WILEY
DOI: 10.1002/eji.200939342
Keywords
MHC class I; Peptide binding; Tapasin
Categories
Funding
- DFG [SP583/2-3]
- Tonjes Vagt Foundation
- German Academic Exchange Service
- Jacobs University
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The 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.
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