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J Exp Med ; 184(5): 2019-24, 1996 Nov 01.
Article in English | MEDLINE | ID: mdl-8920889

ABSTRACT

Human histocompatibility leukocyte antigen (HLA)-DM is a facilitator of antigen presentation via major histocompatibility complex (MHC) class II molecules. In the absence of HLA-DM, MHC class II molecules do not present natural peptides, but tend to remain associated with class II-associated invariant chain peptides (CLIP). Recently, DM was shown to catalyze the release of CLIP from HLA-DR. We have investigated which peptides bound to HLA-DR are vulnerable to release upon encountering DM. By directed substitution of allele-specific anchor residues between CLIP and DR3-cognate peptides and the application of recombinant DM we show that DM catalyzes the release of those peptides bound to HLA-DR3 that do not have appropriate anchor residues and, hence, no optimal ligand binding motif. Thus, HLA-DM acts as a peptide editor, facilitating selection of peptides that stably bind to class II molecules for eventual presentation to the immune system from the pool of available peptides.


Subject(s)
Antigen Presentation , Antigens, Differentiation, B-Lymphocyte/metabolism , HLA-D Antigens/metabolism , HLA-DR3 Antigen/metabolism , Histocompatibility Antigens Class II/metabolism , Peptides/metabolism , Amino Acid Sequence , Binding Sites , Cell Line , HLA-D Antigens/genetics , Humans , Molecular Sequence Data , Protein Binding , Recombinant Proteins/metabolism , Sequence Alignment
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