Production of platelet‐derived growth factor receptor (PDGFR‐β) in E. coli

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Abstract
Portions of the extracellular domain of the platelet‐derived growth factor receptor β (PDGFR‐β) were expressed as fusion proteins with a hexa His tag in E. coli. Following purification by Ni chelate chromatography, the recombinant receptors were tested in cross‐competition studies with 125I‐Iabelled PDGF‐AA and ‐BB. Although of lower affinity than the native receptor (IC50 values of 10−8 M) the recombinant molecules retained ligand binding specificity and neutralised the mitogenic effect of PDGF‐BB. These data indicate that the ligand binding region lies within the first four immunoglobulin‐like domains on PDGFR‐β. This E. coli expression system could be further used as a rapid and economical means to produce mutated receptors and map the ligand binding domain.

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