Bidirectional binding of invariant chain peptides to an MHC class II molecule

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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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