5nu2

Structure of non-fluorescent human urine RBP4

spinqualitylabelsall models 5nu2, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5nu2 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, PLM Related: 5nty Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease [RET4_HUMAN] Defects in RBP4 are a cause of retinol-binding protein deficiency (RBP deficiency) [MIM:180250]. This condition causes night vision problems. It produces a typical 'fundus xerophthalmicus', featuring a progressed atrophy of the retinal pigment epithelium. Function [RET4_HUMAN] Delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin, this prevents its loss by filtration through the kidney glomeruli. Publication Abstract from PubMed RBP4 (plasma retinol-binding protein) is the 21kDa 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 1.5A 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. Human plasma retinol-binding protein (RBP4) is also a fatty acid-binding protein.,Perduca M, Nicolis S, Mannucci B, Galliano M, Monaco HL Biochim Biophys Acta. 2018 Apr;1863(4):458-466. doi:, 10.1016/j.bbalip.2018.01.010. PMID:29414511 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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