5xb1

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'''Unreleased structure'''
 
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The entry 5xb1 is ON HOLD until Paper Publication
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==human ferritin mutant - E-helix deletion==
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<StructureSection load='5xb1' size='340' side='right' caption='[[5xb1]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5xb1]] is a 24 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XB1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XB1 FirstGlance]. <br>
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</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>
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<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=5xb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xb1 OCA], [http://pdbe.org/5xb1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xb1 RCSB], [http://www.ebi.ac.uk/pdbsum/5xb1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xb1 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[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).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5xb1" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Ferroxidase]]
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[[Category: Ahn, B J]]
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[[Category: Hyun, J]]
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[[Category: Jeong, H]]
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[[Category: Jung, Y]]
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[[Category: Kim, H]]
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[[Category: Lee, S G]]
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[[Category: Cage]]
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[[Category: Drug delivery]]
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[[Category: Ferritin]]
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[[Category: Transport protein]]

Revision as of 07:20, 22 February 2018

human ferritin mutant - E-helix deletion

5xb1, resolution 3.00Å

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