 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 3]](xb5027fig3mag.jpg)
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Figure 3
Structural comparison of HLA-A3 and HLA-A2. (a) Superposition of A3–PLP45-53 (blue) and HLA-A2 (orange). HLA-A3 and HLA-A2 show a high degree of equivalence in their α1, α2 and β2m domains. The α3 domains of HLA-A3 and HLA-A2 are also very structurally similar, but the relative position of this domain is subject to a rigid-body shift between molecules. (b) The Cα atoms of residues that differ between HLA-A3 and HLA-A2 are represented as small spheres and coloured cyan if the side chains point into the binding groove in HLA-A3 and dark blue if they do not. The α1 and α2 helices are labelled. (c) Viewed from above the binding groove, PLP45-53 (grey) is shown bound to HLA-A3 (blue) and superposed upon the structure of HLA-A2 (orange). The groove is orientated as in Fig. 3 ![[link]](../../../../../../logos/arrows/d_arr.gif) (b). Polymorphic HLA-A3 residues that differ from HLA-A2 and that contribute to peptide binding are labelled. |
![[Figure 3]](xb5027fig3.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
