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| | <StructureSection load='5nu6' size='340' side='right'caption='[[5nu6]], [[Resolution|resolution]] 1.68Å' scene=''> | | <StructureSection load='5nu6' size='340' side='right'caption='[[5nu6]], [[Resolution|resolution]] 1.68Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5nu6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NU6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5NU6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5nu6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NU6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NU6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.68Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5nty|5nty]], [[5nu2|5nu2]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5nu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nu6 OCA], [http://pdbe.org/5nu6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nu6 RCSB], [http://www.ebi.ac.uk/pdbsum/5nu6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nu6 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5nu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nu6 OCA], [https://pdbe.org/5nu6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nu6 RCSB], [https://www.ebi.ac.uk/pdbsum/5nu6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nu6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/RET4_HUMAN RET4_HUMAN]] Defects in RBP4 are a cause of retinol-binding protein deficiency (RBP deficiency) [MIM:[http://omim.org/entry/180250 180250]]. This condition causes night vision problems. It produces a typical 'fundus xerophthalmicus', featuring a progressed atrophy of the retinal pigment epithelium. | + | [https://www.uniprot.org/uniprot/RET4_HUMAN RET4_HUMAN] Defects in RBP4 are a cause of retinol-binding protein deficiency (RBP deficiency) [MIM:[https://omim.org/entry/180250 180250]. This condition causes night vision problems. It produces a typical 'fundus xerophthalmicus', featuring a progressed atrophy of the retinal pigment epithelium. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RET4_HUMAN 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. | + | [https://www.uniprot.org/uniprot/RET4_HUMAN 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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Galliano, M]] | + | [[Category: Galliano M]] |
| - | [[Category: Monaco, H L]] | + | [[Category: Monaco HL]] |
| - | [[Category: Perduca, M]] | + | [[Category: Perduca M]] |
| - | [[Category: Fatty acid]]
| + | |
| - | [[Category: Lipocalin]]
| + | |
| - | [[Category: Plasma retinol-binding protein]]
| + | |
| - | [[Category: Rbp4]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Perduca M, Nicolis S, Mannucci B, Galliano M, Monaco HL. Human plasma retinol-binding protein (RBP4) is also a fatty acid-binding protein. Biochim Biophys Acta. 2018 Apr;1863(4):458-466. doi:, 10.1016/j.bbalip.2018.01.010. PMID:29414511 doi:http://dx.doi.org/10.1016/j.bbalip.2018.01.010
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