[HTML][HTML] The interplay between citrullination and HLA-DRB1 polymorphism in shaping peptide binding hierarchies in rheumatoid arthritis
The HLA-DRB1 locus is strongly associated with rheumatoid arthritis (RA) susceptibility,
whereupon citrullinated self-peptides bind to HLA-DR molecules bearing the shared epitope
(SE) amino acid motif. However, the differing propensity for citrullinated/non-citrullinated self-
peptides to bind given HLA-DR allomorphs remains unclear. Here, we used a fluorescence
polarization assay to determine a hierarchy of binding affinities of 34 self-peptides
implicated in RA against three HLA-DRB1 allomorphs (HLA-DRB1* 04: 01/* 04: 04/* 04: 05) …
whereupon citrullinated self-peptides bind to HLA-DR molecules bearing the shared epitope
(SE) amino acid motif. However, the differing propensity for citrullinated/non-citrullinated self-
peptides to bind given HLA-DR allomorphs remains unclear. Here, we used a fluorescence
polarization assay to determine a hierarchy of binding affinities of 34 self-peptides
implicated in RA against three HLA-DRB1 allomorphs (HLA-DRB1* 04: 01/* 04: 04/* 04: 05) …