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Tapasin edits peptides on MHC class I molecules by accelerating peptide exchange

✍ Scribed by P. V. K. Praveen; Rakina Yaneva; Hubert Kalbacher; Sebastian Springer

Publisher: John Wiley and Sons
Year: 2009
Tongue: English
Weight: 331 KB
Volume: 40
Category: Article
ISSN: 0014-2980
DOI: 10.1002/eji.200939342

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✦ Synopsis

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.

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