Pathogenicity of Misfolded and Dimeric HLA-B27 Molecules
Figure 2
HLA-B27 structure. (a) Ribbon structure of HLA-B27 heavy chain in association with β2m and peptide. Structurally conserved cysteines at positions 101, 164, 203, and 258 and the unpaired cysteine at p67 are highlighted by Van der Waals radii. (b) Overhead view of the HLA-B27 antigen binding groove highlighting Cys67 and residues (His114, Asp116, Asp77, and Val152) which are polymorphic between the disease-associated HLA-B*2705 and nondisease-associated HLA-B*2706 subtypes. (c) Head on view of the F pocket of the HLA-B27 antigen binding groove. His114 and Asp116 make up the floor of the F pocket, whilst Val152 and Asp77 can contribute to the interaction between HLA-B27 and the carboxy-terminus of the associated peptide. (d) Overhead view of the HLA-B27 antigen binding groove, with Cys67 (Van der Waals radii) and surrounding residues (ball and stick) are depicted, which are unique to HLA-B27 and contribute to the B pocket of HLA-B27.
