Abstract
An association between the MHC class II chaperone molecule Invariant chain (Ii) and MHC class I molecules is known to occur, but the basis of the interaction is undetermined. Evidence is presented here that the CLIP region of Ii is involved in this interaction. A peptide encoding residues 91-99 of CLIP (MRMATPLLM) stabilised multiple MHC class I alleles, with the methionine residue at position 99 having a crucial role in binding to H2-K-b, whereas methionine at position 91 also appeared important in binding to RT1-A(a). Ii can also be detected in the class I MHC peptide loading complex. These data provide an explanation for the association of Ii and MHC class I molecules. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Original language | English |
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Pages (from-to) | 3112-3116 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 580 |
DOIs | |
Publication status | Published - 29 May 2006 |
Keywords
- MHC class I
- invariant chain
- antigen presentation
- peptide loading complex
- MAJOR HISTOCOMPATIBILITY COMPLEX
- CROSS-PRESENTATION
- PEPTIDE-BINDING
- ASSOCIATION
- TAPASIN
- IDENTIFICATION
- SPECIFICITY
- SUBUNITS
- HLA-B27