Conformational variation in structures of classical and non-classical MHCII proteins and functional implications.

Publisher: Blackwell Country of Publication: England NLM ID: 7702118 Publication Model: Print Cited Medium: Internet ISSN: 1600-065X (Electronic) Linking ISSN: 01052896 NLM ISO Abbreviation: Immunol Rev Subsets: MEDLINE

Publication: <2002-> : Oxford : Blackwell
Original Publication: Copenhagen, Munksgaard.

Antigen Presentation*; HLA-D Antigens/*chemistry ; HLA-DR Antigens/*chemistry ; Histocompatibility Antigens Class II/*chemistry ; Peptides/*chemistry; Animals ; Binding Sites ; Crystallography, X-Ray ; HLA-D Antigens/immunology ; HLA-D Antigens/metabolism ; HLA-DR Antigens/immunology ; HLA-DR Antigens/metabolism ; Histocompatibility Antigens Class II/immunology ; Histocompatibility Antigens Class II/metabolism ; Humans ; Hydrogen Bonding ; Mice ; Models, Molecular ; Peptides/immunology ; Peptides/metabolism ; Protein Binding ; Protein Structure, Secondary ; Protein Structure, Tertiary

Recent structural characterizations of classical and non-classical major histocompatibility complex class II (MHCII) proteins have provided a view into the dynamic nature of the MHCII-peptide binding groove and the role that structural changes play in peptide loading processes. Although there have been numerous reports of crystal structures for MHCII-peptide complexes, a detailed analysis comparing all the structures has not been reported, and subtle conformational variations present in these structures may not have been fully appreciated. We compared the 91 MHCII crystal structures reported in the PDB to date, including an HLA-DR mutant particularly susceptible to DM-mediated peptide exchange, and reviewed experimental and computational studies of the effect of peptide binding on MHCII structure. These studies provide evidence for conformational lability in and around the α-subunit 3-10 helix at residues α48-51, a region known to be critical for HLA-DM-mediated peptide exchange. A biophysical study of MHC-peptide hydrogen bond strengths and a recent structure of the non-classical MHCII protein HLA-DO reveal changes in the same region. Conformational variability was observed also in the vicinity of a kink in the β-subunit helical region near residue β66 and in the orientation and loop conformation in the β2 Ig domain. Here, we provide an overview of the regions within classical and non-classical MHCII proteins that display conformational changes and the potential role that these changes may have in the peptide loading/exchange process.
(© 2012 John Wiley & Sons A/S.)

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R01 AI048833 United States AI NIAID NIH HHS; R56 AI038996 United States AI NIAID NIH HHS; R37 AI038996 United States AI NIAID NIH HHS; AI48833 United States AI NIAID NIH HHS; AI38996 United States AI NIAID NIH HHS; R01 AI038996 United States AI NIAID NIH HHS

0 (HLA-D Antigens)
0 (HLA-DO antigens)
0 (HLA-DR Antigens)
0 (Histocompatibility Antigens Class II)
0 (Peptides)

Date Created: 20121011 Date Completed: 20130225 Latest Revision: 20211021

20231215

PMC3471379

10.1111/imr.12003

23046127