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Figure 4.
Figure 4. Implications of UL18 -LIR-1 interaction. (a) View
of D1D2 -HLA-A2 structure with the approximate positions of
potential UL18 glycosylation sites mapped onto the HLA-A2
structure. Potential N-linked glycosylation sites (pink spheres)
are distant from the LIR-1 binding site. The closest predicted
O-linked glycosylation site (gray sphere) is also distant from
the binding site. Three additional O-linked glycosylation sites
are predicted in UL18 in a region corresponding to sequence
between the carboxyl terminus of the HLA-A2 ectodomain and the
transmembrane region. (b) Closer view of the LIR-1 -HLA-A2
interface in the region outlined by the dotted rectangle in a.
The structures of free LIR-1 (ref. 11) and LIR-2 (ref. 17) are
superimposed on the bound LIR-1 structure to show movement of
the loop of residues 76 -84 (mostly disordered in the bound
LIR-1 structure (see Methods). The side chains of LIR-1 Asp80
(which have been linked to the binding of LIR-1 UL18; ref. 11)
and its counterpart in LIR-2, Arg80, are shown as ball-and-stick
representation.
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