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Figure 5.
Figure 5. Space-Filling Representations of the Surface
Character of MIC-A(A and B) A view of the back (A) and the side
(B) of MIC-A highlighting the potential N-linked oligosaccharide
sites present in all primate MIC alleles (orange) and those
conserved in all primate MIC-A alleles (red). Residues shown in
purple correspond to residues buried in a hypothetical complex
with β[2]-m (see Figure 3).(C and D) Views of the equivalent of
the peptide/TCR-binding surface of the platform domain (the
“top,” [C]) and the β[2]-m binding surface of the platform
domain (the “underside,” [D]; same orientation as in [A]) of
MIC-A. Residues conserved across all primate MIC sequences are
colored blue; residues where conservative substitutions have
occurred (L/V/I, E/D, D/N, E/Q, E/N, or R/K) are colored green;
nonconserved residues are colored yellow; residues in the α3
domain are colored gray. Two patches of conserved residues
straddle the N-linked oligosaccharide at Asn-8: patch 1 (below
Asn-8 in [D]): Ser-4, Arg-6, Glu-25, His-27, Gly-30, Gln-31,
Pro-45, Trp-49, Glu-97, and Arg-180; patch 2 (above and to the
left of Asn-8 in [D]); Leu-12, Lys-84, Leu-87, His-109, Tyr-111,
Asp-113, Gly-114, Glu-115, Gln-131, and Ser-132. Residues at
potential N-linked glycosylation sites are colored as in (A) and
(B).
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