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

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 Immunol

authors

Praveen PV,Yaneva R,Kalbacher H,Springer S

doi

10.1002/eji.200939342

subject

Has Abstract

pub_date

2010-01-01 00:00:00

pages

214-24

issue

1

eissn

0014-2980

issn

1521-4141

journal_volume

40

pub_type

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