Recognition of open conformers of classical MHC by chaperones and monoclonal antibodies.

Abstract:

:There is considerable evidence that the conformation and stability of class I and class II major histocompatibility complex (MHC) proteins is dependent upon high-affinity peptide ligation, but structural data for an empty MHC protein unfortunately is lacking. However, several monoclonal antibodies (mAbs) that specifically detect open MHC conformers have been characterized, and they provide insights into the changes associated with peptide loading and unloading. Here, the structural changes make the argument that certain of these open conformer-specific mAbs recognize analogous MHC segments as the molecular chaperones tapasin and DM. MHC residues located in regions flanking the peptide-terminal anchoring pockets have been implicated in both chaperone and monoclonal antibody binding. Indeed, we propose these regions serve as peptide-binding hinges that are uniquely accessible in open MHC.

journal_name

Immunol Rev

journal_title

Immunological reviews

authors

Hansen TH,Lybarger L,Yu L,Mitaksov V,Fremont DH

doi

10.1111/j.0105-2896.2005.00315.x

keywords:

subject

Has Abstract

pub_date

2005-10-01 00:00:00

pages

100-11

eissn

0105-2896

issn

1600-065X

pii

IMR315

journal_volume

207

pub_type

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