Crystallization and preliminary X‐ray diffraction analysis of human phosphate‐binding protein

E-ISSN： 1744-3091|62|1|67-69

ISSN： 1744-3091

Source： Acta Crystallographica Section F, Vol.62, Iss.1, 2006-01, pp. : 67-69

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Abstract

Human phosphate‐binding protein (HPBP) was serendipitously discovered by crystallization and X‐ray crystallography. HPBP belongs to a eukaryotic protein family named DING that is systematically absent from the genomic database. This apoprotein of 38 kDa copurifies with the HDL‐associated apoprotein paraoxonase (PON1) and binds inorganic phosphate. HPBP is the first identified transporter capable of binding phosphate ions in human plasma. Thus, it may be regarded as a predictor of phosphate‐related diseases such as atherosclerosis. In addition, HPBP may be a potential therapeutic protein for the treatment of such diseases. Here, the purification, detergent‐exchange protocol and crystallization conditions that led to the discovery of HPBP are reported.