Crystallization and preliminary X-ray diffraction analysis of human phosphate-binding protein.
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.
Contreras-Martel
Carlos
C
Laboratoire de Cristallogenèse et Cristallographie des Protéines, Institut de Biologie Structurale J.-P. Ebel, 38027 Grenoble, France.
Carpentier
Philippe
P
Morales
Renaud
R
Renault
Frédérique
F
Chesne-Seck
Marie Laure
ML
Rochu
Daniel
D
Masson
Patrick
P
Fontecilla-Camps
Juan Carlos
JC
Chabrière
Eric
E
D001059:Apoproteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D043303:Aryldialkylphosphatase / Q000737:chemistry / Q000302:isolation & purification; D050197:Atherosclerosis / Q000378:metabolism; D008076:Cholesterol, HDL / Q000737:chemistry; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D028061:Phosphate Transport Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism
D001059:Apoproteins; D008076:Cholesterol, HDL; D028061:Phosphate Transport Proteins; D043303:Aryldialkylphosphatase; C468406:PON1 protein, human