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Fig. 1 | Arthritis Research & Therapy

Fig. 1

From: The increased ability to present citrullinated peptides is not unique to HLA-SE molecules: arginine-to-citrulline conversion also enhances peptide affinity for HLA-DQ molecules

Fig. 1

Accommodation of citrulline and arginine residues by HLA-DR4 and HLA-DR3 molecules. a Schematic representation of the peptide-binding pockets of HLA-DR4 and HLA-DR3. Amino acid (AA) residues are color coded according to their properties (white = hydrophilic, gray = hydrophobic, red = acidic, blue = basic). b Competitive binding of a biotin-labeled ApoB peptide with an unlabeled ApoB peptide or ApoB variants with arginine or citrulline residues in p1, p4, p6, p7, and p9 to HLA-DRB1*04:04. c Competitive binding of a biotin-labeled MIF peptide with an unlabeled MIF peptide or MIF variants with arginine or citrulline residues in p1, p4, p6, p7, and p9 to HLA-DRB1*04:05. d Competitive binding of a biotin-labeled myoglobin peptide with an unlabeled myoglobin peptide or myoglobin variants with arginine or citrulline residues in p1, p4, p6, p7, and p9 to HLA-DR3. Graphs depict the IC50 values (μM). ND non-detectable binding. Binding experiments were performed at least three times and plots show pooled experiments. The error bars show the standard error of the mean. *Indicates a p value of <0.05

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Arthritis Research & Therapy

ISSN: 1478-6362

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