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Figure 1 | BMC Structural Biology

Figure 1

From: Crystal structure of LIR-2 (ILT4) at 1.8 Å: differences from LIR-1 (ILT2) in regions implicated in the binding of the Human Cytomegalovirus class I MHC homolog UL18

Figure 1

Purification and characterization of soluble LIR-2 D1D2. A: Size exclusion chromatography of refolded LIR-2 D1D2. Refolded LIR-2 D1D2 elutes from a Superdex 200 column at just before a 13.7 kDa marker protein, consistent with the protein behaving as a compact monomer in solution. The elution volumes of 232, 67 and 13.7 kDa standard proteins are indicated. B: SDS-PAGE analysis of refolded LIR-2. Identical samples of size-exclusion purified LIR-2 D1D2 (~5 μg) were loaded onto a 15% acrylamide SDS gel, under either reducing (R) or non-reducing (NR) conditions. The molecular weights of marker proteins (M) are shown in kilodaltons. Under reducing conditions, LIR-2 migrates in a position consistent with its predicted molecular weight of 22 kDa. Under non-reducing conditions, LIR-2 D1D2 migrates as a single band of higher mobility, suggesting formation of the appropriate disulfide bonds. No higher molecular weight cross-linked species are observed.

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BMC Structural Biology

ISSN: 1472-6807

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