eprintid: 8580
rev_number: 17
eprint_status: archive
userid: 1
dir: disk0/00/00/85/80
datestamp: 2008-07-22 14:52:07
lastmod: 2016-01-20 16:30:23
status_changed: 2012-08-14 15:25:58
type: article
metadata_visibility: show
creators_name: Vogt, Anne B.
creators_name: Stern, Lawrence J.
creators_name: Amshoff, Christine
creators_name: Dobberstein, Bernhard
creators_name: Hämmerling, Günter J.
creators_name: Kropshofer, Harald
title: Interference of Distinct Invariant Chain Regions with Superantigen Contact Area and Antigenic Peptide Binding Groove of HLA-DR
ispublished: pub
subjects: ddc-570
divisions: i-706000
abstract: In the endoplasmic reticulum, MHC class II ab dimers associate with the trimeric invariant chain (li), generating a nine-subunit(abli)3 complex. In the presence of li, the peptide binding groove is blocked, so that loading with self or antigenic peptides can only occur after proteolytic removal of li in specialized post-Golgi compartments. The class 11-associated invariant chain peptide region of li (about residues 81-1 04) is known to mediate binding to class II molecules and blockade of the groove, but this does not exclude additional contact sites for li. Using a set of overlapping li peptides and recombinant soluble li, we demonstrate here that a large segment of Ii encompassing approximately residues 71 to 128 interacts with HLA-DR molecules. The N- and C-terminal regions of this Ii segment appear to bind outside the peptide groove to the contact area for the staphylococcal superantigen Staphylococcus aureus enterotoxin B on the a1 domain. The core region of this segment (residues 95-108)prevents binding of antigenic peptides, probably by interaction with the peptide groove. Occupation of the groove with antigenic peptides abolishes binding not only of the core region, but also that of those Ii peptides that bind outside the groove. These findings suggest the existence of distinct conformational states of class II molecules, with Ii binding preferentially to one form.
abstract_translated_lang: eng
date: 1995
date_type: published
id_scheme: DOI
id_number: 10.11588/heidok.00008580
schriftenreihe_cluster_id: sr-2
schriftenreihe_order: 079
ppn_swb: 1354704053
own_urn: urn:nbn:de:bsz:16-opus-85809
language: eng
bibsort: VOGTANNEBINTERFEREN1995
full_text_status: public
publication: The Journal of Immunology 
volume: 155
pagerange: 4757-4765
citation:   Vogt, Anne B. ; Stern, Lawrence J. ; Amshoff, Christine ; Dobberstein, Bernhard ; Hämmerling, Günter J. ; Kropshofer, Harald  (1995) Interference of Distinct Invariant Chain Regions with Superantigen Contact Area and Antigenic Peptide Binding Groove of HLA-DR.  The Journal of Immunology , 155.  pp. 4757-4765.      
document_url: https://archiv.ub.uni-heidelberg.de/volltextserver/8580/1/Vogt_1995_JImmunol.pdf