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==human ferritin mutant - E-helix deletion==
==human ferritin mutant - E-helix deletion==
<StructureSection load='5yi5' size='340' side='right' caption='[[5yi5]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<SX load='5yi5' size='340' side='right' viewer='molstar' caption='[[5yi5]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5yi5]] is a 24 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YI5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YI5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5yi5]] is a 24 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=5YI5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YI5 FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1] </span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5yi5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yi5 OCA], [http://pdbe.org/5yi5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yi5 RCSB], [http://www.ebi.ac.uk/pdbsum/5yi5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yi5 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=5yi5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yi5 OCA], [https://pdbe.org/5yi5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yi5 RCSB], [https://www.ebi.ac.uk/pdbsum/5yi5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yi5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/FRIH_HUMAN FRIH_HUMAN]] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. 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).
[https://www.uniprot.org/uniprot/FRIH_HUMAN FRIH_HUMAN] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. 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;">
== Publication Abstract from PubMed ==
Human ferritins are emerging platforms for non-toxic protein-based drug delivery, owing to their intrinsic or acquirable targeting abilities to cancer cells and hollow cage structures for drug loading. However, reliable strategies for high-level drug encapsulation within ferritin cavities and prompt cellular drug release are still lacking. Ferritin nanocages were developed with partially opened hydrophobic channels, which provide stable routes for spontaneous and highly accumulated loading of Fe(II) -conjugated drugs as well as pH-responsive rapid drug release at endoplasmic pH. Multiple cancer-related compounds, such as doxorubicin, curcumin, and quercetin, were actively and heavily loaded onto the prepared nicked ferritin. Drugs on these minimally modified ferritins were effectively delivered inside cancer cells with high toxicity.


Four-fold Channel-Nicked Human Ferritin Nanocages for Active Drug Loading and pH-Responsive Drug Release.,Ahn B, Lee SG, Yoon HR, Lee JM, Oh HJ, Kim HM, Jung Y Angew Chem Int Ed Engl. 2018 Jan 23. doi: 10.1002/anie.201800516. PMID:29359486<ref>PMID:29359486</ref>
==See Also==
 
*[[Ferritin 3D structures|Ferritin 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5yi5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</SX>
[[Category: Ferroxidase]]
[[Category: Homo sapiens]]
[[Category: Ahn, B J]]
[[Category: Large Structures]]
[[Category: Hyun, J]]
[[Category: Ahn BJ]]
[[Category: Jeong, H]]
[[Category: Hyun J]]
[[Category: Jung, Y]]
[[Category: Jeong H]]
[[Category: Kim, H]]
[[Category: Jung Y]]
[[Category: Lee, S G]]
[[Category: Kim H]]
[[Category: Yoon, H R]]
[[Category: Lee SG]]
[[Category: Cage]]
[[Category: Yoon HR]]
[[Category: Drug delivery]]
[[Category: Ferritin]]
[[Category: Transport protein]]

Latest revision as of 10:23, 27 March 2024

human ferritin mutant - E-helix deletion

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