Figure 2 - full size

 

Figure 2.
Figure 2. Crystal Structure of HLA-DR1 Bound to AAYSDQATPLLLSPR(A) 2Fo-Fc electron density map contoured at 1σ using data in the resolution rage of 30–2.4 Å, with all peptide atoms omitted from the map calculation. The peptide carbon atoms are yellow, and nitrogen and oxygen atoms are blue and red, respectively.(B) The AAYSDQATPLLLSPR peptide from the HLA-DR1/SEC3-3B2 complex (carbon atoms colored in yellow) was superimposed with the peptides present in the structure of HLA-DR1 without the superantigen (carbon atoms colored in green or magenta for the two molecules in the asymmetric unit).(C) 2Fo-Fc electron density maps contoured at 1σ for the P10 region of HLA-DR1/AAYSDQATPLLLSPR. (All the labeled residues were omitted from the map calculation). The carbon atoms for the peptide are yellow, and the ones for HLA-DR1 are green. The view is from the right side of (A), with the α subunit helix to the right and the β subunit helix to the left.(D) Surface of the HLA-DR1 P10 region shown with the same view as (C). Residues lining the pocket are labeled. Residues β57 and β60 are polymorphic among HLA-DR proteins. Figures were generated with PyMol [43].

The above figure is reprinted by permission from Cell Press: Chem Biol (2004, 11, 1395-1402) copyright 2004.