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Figure 1.
Figure 1. LIR-1 D1D2 Crystal Structure(A) Ribbon diagram of
the structure of LIR-1 D1D2. Disulfide bonds are shown in
yellow, and dashed lines indicate disordered loops. Arrow
indicates the location of the bond between residues 99 and 100,
which can be proteolitically cleaved to generate stable
fragments corresponding to D1 and D2 ([10]).(B) Topology diagram
of LIR-1 D1D2. β strands are blue, 3[10] helices are green, and
polyproline type II helices are red.(C) Stereoview of LIR-1 D1
(green) superimposed upon KIR2DL1 ([16]) (red). N and C termini
of LIR-1 D1D2 are labeled. Cα atoms of the D1 domains of each
structure were superimposed, illustrating the slight
displacement of the D2 domains. Root mean square deviation
(r.m.s.d) values for superpositions: 0.92 Å (71 Cα atoms)
(LIR-1 D1 and KIR2DL1 D1), 1.25 Å (88 Cα atoms) (LIR-1 D2
and KIR2DL1 D2), 1.36 Å (67 Cα atoms) (LIR-1 D1 and LIR-1
D2).(D) LIR-1 D1D2 model in the region of the D1 3[10] helix
superimposed on a 2.1 Å 2|F[obs]| − |F[calc]| annealed
omit electron density map contoured at 1.0σ (map radius, 3.5
Å).
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