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Figure 3.
Crystallographic structure of HLA-A2-VLH at 1.3Å. (A)
Overall structure of HLA-A2-VLH complex, with heavy chain
(gray), β2m (cyan), and VLH peptide (blue) shown. (B) 2Fo-Fc
electron density for the VLH peptide, with primary anchors and
P3 to P5 highlighted. (C) Structure of the VLH mHag in the
HLA-A2-antigen binding groove, with antigen-binding pockets A to
F indicated, and VLH peptide surface indicated in green. The
structure highlights relatively poor contacts with pockets E and
F. (D) Orientation of H3 in and around the D pocket. H3 packs
snugly against the walls of the D pocket, maintaining van der
Waal's contacts with Tyr-159, Leu-156, and Gln-155, and also to
Asp-4 of the peptide. It is also participates in a
hydrogen-bonding network to Gln-155, and peptide residues Asp-4
and Asp-5, via ordered water molecules. Semitransparent peptide
surface shown in green.
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