4dyx: Difference between revisions
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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=4dyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dyx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dyx RCSB], [http://www.ebi.ac.uk/pdbsum/4dyx PDBsum]</span></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=4dyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dyx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dyx RCSB], [http://www.ebi.ac.uk/pdbsum/4dyx PDBsum]</span></td></tr> | ||
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== 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). | |||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 02:33, 25 December 2014
Crystal Structure of the Cu-adduct of Human H-Ferritin variant 4His-delta C-starCrystal Structure of the Cu-adduct of Human H-Ferritin variant 4His-delta C-star
Structural highlights
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 PubMedThe ability to chemically control protein-protein interactions would allow the interrogation of dynamic cellular processes and lead to a better understanding and exploitation of self-assembling protein architectures. Here we introduce a new engineering strategy-reverse metal-templated interface redesign (rMeTIR)-that transforms a natural protein-protein interface into one that only engages in selective response to a metal ion. We have applied rMeTIR to render the self-assembly of the cage-like protein ferritin controllable by divalent copper binding, which has allowed the study of the structure and stability of the isolated ferritin monomer, the demonstration of the primary role of conserved hydrogen-bonding interactions in providing geometric specificity for cage assembly and the uniform chemical modification of the cage interior under physiological conditions. Notably, copper acts as a structural template for ferritin assembly in a manner that is highly reminiscent of RNA sequences that template virus capsid formation. Re-engineering protein interfaces yields copper-inducible ferritin cage assembly.,Huard DJ, Kane KM, Tezcan FA Nat Chem Biol. 2013 Jan 20. doi: 10.1038/nchembio.1163. PMID:23340339[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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