 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 1]](xb5027fig1mag.jpg)
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Figure 1
The crystal structure of A3–PLP45-53. (a) The view is from above into the binding groove of A3–PLP45-53. The MHC heavy chain is shown in blue and the peptide PLP45-53 in red. σA-weighted Fo − Fc electron density for the peptide PLP45-53 (generated in PHENIX after deletion of the peptide followed by simulated annealing to minimize model bias) is also shown contoured at 2.7σ. (b) Characteristics of the HLA-A3 peptide-binding groove. View from above into the binding groove of HLA-A3. The side chains of individual MHC heavy-chain residues involved in peptide binding are shown as sticks and labelled. The schematic inset provides a key to the locations of the canonical pockets A–F. |
![[Figure 1]](xb5027fig1.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
