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Determination of the HLA-DM interaction site on HLA-DR molecules.

Abstract：

:HLA-DM removes CLIP and other loosely bound peptides from MHC class II molecules. The crystal structures of class II molecules and of HLA-DM have not permitted identification of their interaction sites. Here, we describe mutations in class II that impair interactions with DM. Libraries of randomly mutagenized DR3 alpha and beta chains were screened for their ability to cause cell surface accumulation of CLIP/DR3 complexes in EBV-B cells. Seven mutations were associated with impaired peptide loading in vivo, as detected by SDS stability assays. In vitro, these mutant DR3 molecules were resistant to DM-catalyzed CLIP release and showed reduced binding to DM. All mutations localize to a single lateral face of HLA-DR, which we propose interacts with DM during peptide exchange.

journal_name

Immunity

journal_title

Immunity

authors

Doebele RC,Busch R,Scott HM,Pashine A,Mellins ED

doi

10.1016/s1074-7613(00)00051-0

keywords:

subject

Has Abstract

pub_date

2000-10-01 00:00:00

pages

517-27

issue

4

eissn

1074-7613

issn

1097-4180

pii

S1074-7613(00)00051-0

journal_volume

13

pub_type

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