Abstract:
: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.
journal_name
Eur J Immunoljournal_title
European journal of immunologyauthors
Praveen PV,Yaneva R,Kalbacher H,Springer Sdoi
10.1002/eji.200939342subject
Has Abstractpub_date
2010-01-01 00:00:00pages
214-24issue
1eissn
0014-2980issn
1521-4141journal_volume
40pub_type
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