5yi5: Difference between revisions

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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=''>
<StructureSection load='5yi5' size='340' side='right'caption='[[5yi5]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5yi5]] is a 24 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://en.wikipedia.org/wiki/Human Human]. 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>
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</div>
</div>
<div class="pdbe-citations 5yi5" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5yi5" style="background-color:#fffaf0;"></div>
==See Also==
*[[Ferritin 3D structures|Ferritin 3D structures]]
== References ==
== References ==
<references/>
<references/>
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[[Category: Ferroxidase]]
[[Category: Ferroxidase]]
[[Category: Human]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Ahn, B J]]
[[Category: Ahn, B J]]
[[Category: Hyun, J]]
[[Category: Hyun, J]]

Revision as of 10:29, 6 November 2019

human ferritin mutant - E-helix deletionhuman ferritin mutant - E-helix deletion

Structural highlights

5yi5 is a 24 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:FTH1, FTH, FTHL6, OK/SW-cl.84, PIG15 (HUMAN)
Activity:Ferroxidase, with EC number 1.16.3.1
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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).

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Ahn B, Lee SG, Yoon HR, Lee JM, Oh HJ, Kim HM, Jung Y. Four-fold Channel-Nicked Human Ferritin Nanocages for Active Drug Loading and pH-Responsive Drug Release. Angew Chem Int Ed Engl. 2018 Jan 23. doi: 10.1002/anie.201800516. PMID:29359486 doi:http://dx.doi.org/10.1002/anie.201800516

5yi5, resolution 3.00Å

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OCA