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| Item Type: | Article |
|---|---|
| Title: | Bidirectional binding of invariant chain peptides to an MHC class II molecule |
| Creators Name: | Guenther, S., Schlundt, A., Sticht, J., Roske, Y., Heinemann, U., Wiesmueller, K.H., Jung, G., Falk, K., Roetzschke, O. and Freund, C. |
| Abstract: | T-cell recognition of peptides bound to MHC class II (MHCII) molecules is a central event in cell-mediated adaptive immunity. The current paradigm holds that prebound class II-associated invariant chain peptides (CLIP) and all subsequent antigens maintain a canonical orientation in the MHCII binding groove. Here we provide evidence for MHCII-bound CLIP inversion. NMR spectroscopy demonstrates that the interconversion from the canonical to the inverse alignment is a dynamic process, and X-ray crystallography shows that conserved MHC residues form a hydrogen bond network with the peptide backbone in both orientations. The natural catalyst HLA-DM accelerates peptide reorientation and the exchange of either canonically or inversely bound CLIP against antigenic peptide. Thus, noncanonical MHC-CLIP displays the hallmarks of a structurally and functionally intact antigen-presenting complex. |
| Keywords: | Bidirectional Binding, Antigen Presentation, Peptide Loading |
| Source: | Proceedings of the National Academy of Sciences of the United States of America |
| ISSN: | 0027-8424 |
| Publisher: | National Academy of Sciences |
| Volume: | 107 |
| Number: | 51 |
| Page Range: | 22219-22224 |
| Date: | 21 December 2010 |
| Official Publication: | https://doi.org/10.1073/pnas.1014708107 |
| PubMed: | View item in PubMed |
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