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Figure 5.
Figure 5 The putative carbohydrate-binding pocket at the
Ly49A/H-2D^d interface. A close-up of the complex interface at
site 1 is shown, centred at the open cavity around N176, a
conserved glycosylation site in rodent MHC-I molecules. The
orientation and the polypeptide chain representation are as in
Fig. 1b. Two proximal carbohydrates, a GlcNAc and a fucose
residue, have been modelled on the basis of crystal structures
of MHC-I molecules deposited in the Protein Data Bank. The
carbohydrate residues (pink) and surrounding amino-acid side
chains (cyan for Ly49A and yellow for H-2D^d) are shown in
ball-and-stick representation; the branching fucose residue
could fit well into the deep open pocket. The red arrow
indicates position 4 in the GluNAc residue where the rest of the
oligosaccharide is attached, and which can establish further
interactions along the flat surface of the Ly49A dimer (Fig. 1b).
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