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Human Plasma Retinol-Binding Protein (RBP4) Is Also a Fatty Acid-Binding Protein

Human Plasma Retinol-Binding Protein (RBP4) Is Also a Fatty Acid-Binding Protein

Massimiliano Perduca, Stefania Nicolis, Barbara Mannucci, Monica Galliano, Hugo L Monaco

Biochim Biophys Acta Mol Cell Biol Lipids. 2018 Apr;1863(4):458-466.

PMID: 29414511

Abstract:

RBP4 (plasma retinol-binding protein) is the 21 kDa transporter of all-trans retinol that circulates in plasma as a moderately tight 1:1 molar complex of the vitamin with the protein. RBP4 is primarily synthesized in the liver but is also produced by adipose tissue and circulates bound to a larger protein, transthyretin, TTR, that serves to increase its molecular mass and thus avoid its elimination by glomerular filtration. This paper reports the high resolution three-dimensional structures of human RBP4 naturally lacking bound retinol purified from plasma, urine and amniotic fluid. In all these crystals we found a fatty acid molecule bound in the hydrophobic ligand-binding site, a result confirmed by mass spectrometry measurements. In addition we also report the 1.5 Å resolution structures of human holo-RBP4 and of the protein saturated with palmitic and lauric acid and discuss the interaction of the fatty acids and retinol with the protein.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42413141	RBP4 human			Price

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