5erk

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m (Protected "5erk" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5erk is ON HOLD
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==X-ray structure of horse spleen apoferritin (control)==
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<StructureSection load='5erk' size='340' side='right' caption='[[5erk]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5erk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ERK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ERK FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5erk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5erk OCA], [http://pdbe.org/5erk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5erk RCSB], [http://www.ebi.ac.uk/pdbsum/5erk PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://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).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cisplatin (CDDP) can be encapsulated within the central cavity of reconstituted (apo)ferritin, (A)Ft, to form a drug-loaded protein of potential great interest for targeted cancer treatments. In this study, the interactions occurring between cisplatin and native horse spleen Ft in CDDP-encapsulated AFt are investigated by high-resolution X-ray crystallography. A protein bound Pt center is unambiguously identified in AFt subunits by comparative analysis of difference Fourier electron density maps and of anomalous dispersion data. Indeed, a [Pt(NH3)2H2O]2+ fragment is found coordinated to the His132 residue located on the inner surface of the large AFt spherical cage. Remarkably, Pt binding does not alter the overall physicochemical features (shape, volume, polarity/hydrophobicity and electrostatic potential) of the outer surface of the AFt nanocage. CDDP-encapsulated AFt appears to be an ideal nanocarrier for CDDP delivery to target sites, as it possesses high biocompatibility and can be internalized by receptor mediated endocytosis, thus carrying the drug to tumor tissue with higher selectivity than free CDDP.
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Authors: Pontillo, N., Merlino, A.
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Cisplatin encapsulation within a ferritin nanocage: a high-resolution crystallographic study.,Pontillo N, Pane F, Messori L, Amoresano A, Merlino A Chem Commun (Camb). 2016 Feb 18. PMID:26888424<ref>PMID:26888424</ref>
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Description: X-ray structure of horse spleen apoferritin (control)
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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 5erk" 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: Equus caballus]]
[[Category: Merlino, A]]
[[Category: Merlino, A]]
[[Category: Pontillo, N]]
[[Category: Pontillo, N]]
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[[Category: Metal transport]]
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[[Category: Protein nanocage]]

Revision as of 15:02, 2 March 2016

X-ray structure of horse spleen apoferritin (control)

5erk, resolution 2.00Å

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