Crystal Structure of a CD163 Scavenger Receptor Cysteine-rich Domain Produced in Pichia Pastoris

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CD163 is an endocytic receptor specifically expressed in monocytes/macrophages and belongs to class B of the scavenger receptor cysteine-rich(SRCR) superfamily(SRCR-SF). It plays critical roles in various physiological and pathological pathways. In this study, the fifth SRCR domain(SRCR5) of porcine CD163(pCD163) was expressed in Pichia pastoris system. The recombinant protein was homogeneous after purification by metal-affinity and size-exclusion chromatography. The purified protein was then assayed for its biological function. Single crystals of pCD163 SRCR5 were obtained under the condition of 25% PEG 4000, 0.1 M citric acid pH_3.5 and its structure was finally determined at 1.80 ?. All these results provide functional pCD163 SRCR5 in large quantity for future research, and enrich the structural details for CD163 and the SRCR-SF. CD 163 is an endocytic receptor specifically expressed in monocytes / macrophages and belongs to class B of the scavenger receptor cysteine-rich (SRCR) superfamily (SRCR-SF). It plays critical roles in various physiological and pathological pathways. In this study, the fifth The recombinant protein was then after purification by metal-affinity and size-exclusion chromatography. The purified protein was then assayed for its biological function. Single crystals of pCD163 (pCD163) was expressed in Pichia pastoris system. SRCR5 was obtained under the condition of 25% PEG 4000, 0.1 M citric acid pH_3.5 and its structure was finally determined at 1.80 ?. All these results provide functional pCD163 SRCR5 in large quantity for future research, and enrich the structural details for CD163 and the SRCR-SF.
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