The mechanism of action of tapasin in the peptide exchange on MHC class I molecules determined from kinetics simulation studies.

Abstract:

:To understand the mechanism of action of the chaperone protein tapasin, which mediates loading of high-affinity peptides onto major histocompatibility complex (MHC) class I molecules in the antiviral immune response, we have performed numerical simulations of the class I-peptide binding process with four different mechanistic hypotheses from the literature, and tested our predictions by laboratory experiments. We find - in agreement of experimental and theoretical studies - that class I-peptide binding in cells is generally under kinetic control, and that tapasin introduces partial thermodynamic control to the process by competing with peptide for binding to class I. Based on our results, we suggest further experimental directions.

journal_name

Mol Immunol

journal_title

Molecular immunology

authors

Schneeweiss C,Garstka M,Smith J,Hütt MT,Springer S

doi

10.1016/j.molimm.2009.02.032

subject

Has Abstract

pub_date

2009-06-01 00:00:00

pages

2054-63

issue

10

eissn

0161-5890

issn

1872-9142

pii

S0161-5890(09)00108-4

journal_volume

46

pub_type

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