5h9a: Difference between revisions
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<StructureSection load='5h9a' size='340' side='right'caption='[[5h9a]], [[Resolution|resolution]] 1.38Å' scene=''> | <StructureSection load='5h9a' size='340' side='right'caption='[[5h9a]], [[Resolution|resolution]] 1.38Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5h9a]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5h9a]] 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=5H9A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H9A 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]] 1.381Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene></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=5h9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h9a OCA], [https://pdbe.org/5h9a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h9a RCSB], [https://www.ebi.ac.uk/pdbsum/5h9a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h9a ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/RET1_HUMAN RET1_HUMAN] Intracellular transport of retinol. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Retinol-binding protein|Retinol-binding protein]] | *[[Retinol-binding protein 3D structures|Retinol-binding protein 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Arne | [[Category: Arne JM]] | ||
[[Category: Banerjee | [[Category: Banerjee S]] | ||
[[Category: Golczak | [[Category: Golczak M]] | ||
[[Category: Kiser | [[Category: Kiser PD]] | ||
[[Category: Silvaroli | [[Category: Silvaroli JA]] | ||
Latest revision as of 10:27, 9 August 2023
Crystal structure of the Apo form of human cellular retinol binding protein 1Crystal structure of the Apo form of human cellular retinol binding protein 1
Structural highlights
FunctionRET1_HUMAN Intracellular transport of retinol. Publication Abstract from PubMedImportant in regulating the uptake, storage, and metabolism of retinoids, cellular retinol-binding protein 1 (CRBP1) is essential for trafficking vitamin A through the cytoplasm. However, the molecular details of ligand uptake and targeted release by CRBP1 remain unclear. Here we report the first structure of CRBP1 in a ligand-free form as well as ultra-high resolution structures of this protein bound to either all-trans-retinol or retinylamine, the latter a therapeutic retinoid that prevents light-induced retinal degeneration. Superpositioning of human apo- and holo-CRBP1 revealed major differences within segments surrounding the entrance to the retinoid-binding site. These included alpha-helix II and hairpin turns between beta-strands betaC-betaD and betaE-betaF as well as several side chains, such as Phe-57, Tyr-60, and Ile-77, that change their orientations to accommodate the ligand. Additionally, we mapped hydrogen bond networks inside the retinoid-binding cavity and demonstrated their significance for the ligand affinity. Analyses of the crystallographic B-factors indicated several regions with higher backbone mobility in the apoprotein that became more rigid upon retinoid binding. This conformational flexibility of human apo-CRBP1 facilitates interaction with the ligands, whereas the more rigid holoprotein structure protects the labile retinoid moiety during vitamin A transport. These findings suggest a mechanism of induced fit upon ligand binding by mammalian cellular retinol-binding proteins. Ligand Binding Induces Conformational Changes in Human Cellular Retinol-binding Protein 1 (CRBP1) Revealed by Atomic Resolution Crystal Structures.,Silvaroli JA, Arne JM, Chelstowska S, Kiser PD, Banerjee S, Golczak M J Biol Chem. 2016 Apr 15;291(16):8528-40. doi: 10.1074/jbc.M116.714535. Epub 2016, Feb 21. PMID:26900151[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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