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

ABSTRACT: 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 st

SUBMITTER: Painter CA 

PROVIDER: S-EPMC3471379 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature