5nu7: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='5nu7' size='340' side='right'caption='[[5nu7]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='5nu7' size='340' side='right'caption='[[5nu7]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5nu7]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5nu7]] 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=5NU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NU7 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> | ||
<tr id=' | <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=RTL:RETINOL'>RTL</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5nu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nu7 OCA], [https://pdbe.org/5nu7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nu7 RCSB], [https://www.ebi.ac.uk/pdbsum/5nu7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nu7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
[ | [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 == | ||
[ | [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 == | ||
| Line 30: | Line 30: | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Galliano | [[Category: Galliano M]] | ||
[[Category: Monaco | [[Category: Monaco HL]] | ||
[[Category: Perduca | [[Category: Perduca M]] | ||
Latest revision as of 15:08, 22 November 2023
Structure of human holo plasma RBP4Structure of human holo plasma RBP4
Structural highlights
DiseaseRET4_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. FunctionRET4_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 PubMedRBP4 (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 AlsoReferences
|
| ||||||||||||||||||