Empty Class II Major Histocompatibility Complex Created by Peptide Photolysis Establishes the Role of DM in Peptide Association-Reference-Cited by-同舟云学术

Empty Class II Major Histocompatibility Complex Created by Peptide Photolysis Establishes the Role of DM in Peptide Association

Published:2007-07 Issue:29 Volume:282 Page:21425-21436
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Grotenbreg Gijsbert M.,Nicholson Melissa J.,Fowler Kevin D.,Wilbuer Kathrin,Octavio Leah,Yang Maxine,Chakraborty Arup K.,Ploegh Hidde L.,Wucherpfennig Kai W.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference42 articles.

1. Invariant chain association with HLA-DR molecules inhibits immunogenic peptide binding

2. MHC class II-associated invariant chain contains a sorting signal for endosomal compartments

3. HLA-DR molecules from an antigen-processing mutant cell line are associated with invariant chain peptides

4. The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3

5. The MHC class II-associated invariant chain-derived peptide CLIP binds to the peptide-binding groove of class II molecules

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