5ix6: Difference between revisions
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<StructureSection load='5ix6' size='340' side='right'caption='[[5ix6]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='5ix6' size='340' side='right'caption='[[5ix6]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ix6]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5ix6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IX6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IX6 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AU:GOLD+ION'>AU</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AU:GOLD+ION'>AU</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5ix6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ix6 OCA], [https://pdbe.org/5ix6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ix6 RCSB], [https://www.ebi.ac.uk/pdbsum/5ix6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ix6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/FRIL_HORSE FRIL_HORSE] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ferraro | [[Category: Ferraro G]] | ||
[[Category: Merlino | [[Category: Merlino A]] | ||
[[Category: Pontillo | [[Category: Pontillo N]] | ||
Latest revision as of 13:36, 6 September 2023
X-ray structure of Auoxo3-encapsulated horse spleen apoferritinX-ray structure of Auoxo3-encapsulated horse spleen apoferritin
Structural highlights
FunctionFRIL_HORSE Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity). Publication Abstract from PubMedAuoxo3, a cytotoxic gold(iii) compound, was encapsulated within a ferritin nanocage. Inductively coupled plasma mass spectrometry, circular dichroism, UV-Vis absorption spectroscopy and X-ray crystallography confirm the potential-drug encapsulation. The structure shows that naked Au(i) ions bind to the side chains of Cys48, His49, His114, His114 and Cys126, Cys126, His132, His147. The gold-encapsulated nanocarrier has a cytotoxic effect on different aggressive human cancer cells, whereas it is significantly less cytotoxic for non-tumorigenic cells. Gold-based drug encapsulation within a ferritin nanocage: X-ray structure and biological evaluation as a potential anticancer agent of the Auoxo3-loaded protein.,Ferraro G, Monti DM, Amoresano A, Pontillo N, Petruk G, Pane F, Cinellu MA, Merlino A Chem Commun (Camb). 2016 Jun 21. PMID:27326513[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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