Dipeptides catalyze rapid peptide exchange on MHC class I molecules.

Abstract:

:Peptide ligand selection by MHC class I molecules, which occurs by iterative optimization, is the centerpiece of immunodominance in antiviral and antitumor immune responses. For its understanding, the molecular mechanisms of peptide binding and dissociation by class I molecules must be elucidated. To this end, we have investigated dipeptides that bind to the F pocket of class I molecules. We find that they accelerate the dissociation of prebound peptides of both low and high affinity, suggesting a mechanism of action for the peptide-exchange chaperone tapasin. Peptide exchange on class I molecules also has practical uses in epitope discovery and T-cell monitoring.

authors

Saini SK,Schuster H,Ramnarayan VR,Rammensee HG,Stevanović S,Springer S

doi

10.1073/pnas.1418690112

subject

Has Abstract

pub_date

2015-01-06 00:00:00

pages

202-7

issue

1

eissn

0027-8424

issn

1091-6490

pii

1418690112

journal_volume

112

pub_type

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