4dyz - Revision history

OCA at 14:48, 14 March 2024

OCA — Thu, 14 Mar 2024 14:48:10 GMT

←Older revision		Revision as of 14:48, 14 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4dyz]] is a 1 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=4DYZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DYZ FirstGlance]. <br>		<table><tr><td colspan='2'>[[4dyz]] is a 1 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=4DYZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DYZ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.3Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></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=4dyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dyz OCA], [https://pdbe.org/4dyz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dyz RCSB], [https://www.ebi.ac.uk/pdbsum/4dyz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dyz 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=4dyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dyz OCA], [https://pdbe.org/4dyz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dyz RCSB], [https://www.ebi.ac.uk/pdbsum/4dyz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dyz ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[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).	+	[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 ==~~	+
-	The 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<ref>PMID:23340339</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4dyz" style="background-color:#fffaf0;"></div>~~	+

	==See Also==		==See Also==
	*[[Ferritin 3D structures\|Ferritin 3D structures]]		*[[Ferritin 3D structures\|Ferritin 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 08:44, 21 September 2022

OCA — Wed, 21 Sep 2022 08:44:29 GMT

←Older revision		Revision as of 08:44, 21 September 2022
Line 1:		Line 1:

	==Crystal Structure of the apo form of Human H-Ferritin variant MIC1==		==Crystal Structure of the apo form of Human H-Ferritin variant MIC1==
-	<StructureSection load='4dyz' size='340' side='right' caption='[[4dyz]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='4dyz' size='340' side='right'caption='[[4dyz]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4dyz]] is a 1 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=4DYZ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4DYZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4dyz]] is a 1 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=4DYZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DYZ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2cei\|2cei]], [[4dyx\|4dyx]], [[4dyy\|4dyy]], [[4dz0\|4dz0]]</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=4dyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dyz OCA], [https://pdbe.org/4dyz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dyz RCSB], [https://www.ebi.ac.uk/pdbsum/4dyz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dyz ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FTH1, FTH, FTHL6, OK/SW-cl.84, PIG15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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>	+
-	<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=4dyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dyz OCA], [~~http~~://pdbe.org/4dyz PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4dyz RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4dyz PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4dyz 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;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 20:

	==See Also==		==See Also==
-	*[[Ferritin\|Ferritin]]	+	*[[Ferritin 3D structures\|Ferritin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Ferroxidase~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Human~~]]	+	[[Category: Large Structures]]
-	[[Category: Huard~~, D J.E~~]]	+	[[Category: Huard DJE]]
-	[[Category: Tezcan~~, F A]]~~	+	[[Category: Tezcan FA]]
-	~~[[Category: Four-helix bundle]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 07:22, 4 August 2016

OCA — Thu, 04 Aug 2016 07:22:32 GMT

←Older revision		Revision as of 07:22, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of the apo form of Human H-Ferritin variant MIC1==		==Crystal Structure of the apo form of Human H-Ferritin variant MIC1==
	<StructureSection load='4dyz' size='340' side='right' caption='[[4dyz]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='4dyz' size='340' side='right' caption='[[4dyz]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4dyz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DYZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DYZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4dyz]] is a 1 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=4DYZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DYZ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2cei\|2cei]], [[4dyx\|4dyx]], [[4dyy\|4dyy]], [[4dz0\|4dz0]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2cei\|2cei]], [[4dyx\|4dyx]], [[4dyy\|4dyy]], [[4dz0\|4dz0]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FTH1, FTH, FTHL6, OK/SW-cl.84, PIG15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FTH1, FTH, FTHL6, OK/SW-cl.84, PIG15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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>		<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>
-	<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=4dyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dyz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dyz RCSB], [http://www.ebi.ac.uk/pdbsum/4dyz 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=4dyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dyz OCA], [http://pdbe.org/4dyz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dyz RCSB], [http://www.ebi.ac.uk/pdbsum/4dyz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dyz ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4dyz" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 27:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Ferroxidase]]		[[Category: Ferroxidase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Huard, D J.E]]		[[Category: Huard, D J.E]]
	[[Category: Tezcan, F A]]		[[Category: Tezcan, F A]]
	[[Category: Four-helix bundle]]		[[Category: Four-helix bundle]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 06:52, 25 December 2014

OCA — Thu, 25 Dec 2014 06:52:58 GMT

←Older revision		Revision as of 06:52, 25 December 2014
Line 9:		Line 9:
	<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=4dyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dyz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dyz RCSB], [http://www.ebi.ac.uk/pdbsum/4dyz 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=4dyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dyz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dyz RCSB], [http://www.ebi.ac.uk/pdbsum/4dyz PDBsum]</span></td></tr>
	</table>		</table>
		+	== 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).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 14:29, 9 December 2014

OCA — Tue, 09 Dec 2014 14:29:48 GMT

←Older revision		Revision as of 14:29, 9 December 2014
Line 1:		Line 1:
-	[[~~Image:~~4dyz.~~png~~\|~~left~~\|~~200px~~]]	+	==Crystal Structure of the apo form of Human H-Ferritin variant MIC1==
		+	<StructureSection load='4dyz' size='340' side='right' caption='[[4dyz]], [[Resolution\|resolution]] 2.30Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4dyz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DYZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DYZ FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2cei\|2cei]], [[4dyx\|4dyx]], [[4dyy\|4dyy]], [[4dz0\|4dz0]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FTH1, FTH, FTHL6, OK/SW-cl.84, PIG15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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>
		+	<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=4dyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dyz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dyz RCSB], [http://www.ebi.ac.uk/pdbsum/4dyz PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The 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.

-	~~{{STRUCTURE_4dyz\| PDB=4dyz \| SCENE= }}~~	+	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<ref>PMID:23340339</ref>

-	~~===Crystal Structure~~ of the ~~apo form~~ of ~~Human H-Ferritin variant MIC1===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_23340339}}~~	+	==See Also==
-		+	*[[Ferritin\|Ferritin]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~4dyz~~]] ~~is a 1 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DYZ OCA].~~	+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Ferroxidase]]		[[Category: Ferroxidase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Huard, D J.E.]]	+	[[Category: Huard, D J.E]]
-	[[Category: Tezcan, F A.]]	+	[[Category: Tezcan, F A]]
	[[Category: Four-helix bundle]]		[[Category: Four-helix bundle]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 09:25, 13 February 2013

OCA — Wed, 13 Feb 2013 09:25:33 GMT

←Older revision		Revision as of 09:25, 13 February 2013
Line 1:		Line 1:
-	[[Image:4dyz.~~jpg~~\|left\|200px]]	+	[[Image:4dyz.png\|left\|200px]]

	{{STRUCTURE_4dyz\| PDB=4dyz \| SCENE= }}		{{STRUCTURE_4dyz\| PDB=4dyz \| SCENE= }}
Line 5:		Line 5:
	===Crystal Structure of the apo form of Human H-Ferritin variant MIC1===		===Crystal Structure of the apo form of Human H-Ferritin variant MIC1===

		+	{{ABSTRACT_PUBMED_23340339}}

	==About this Structure==		==About this Structure==

OCA at 11:57, 23 January 2013

OCA — Wed, 23 Jan 2013 11:57:56 GMT

←Older revision		Revision as of 11:57, 23 January 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4dyz.jpg\|left\|200px]]

-	~~The entry~~ 4dyz ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_4dyz\| PDB=4dyz \| SCENE= }}

-	~~Authors: Tezcan, F.A., Huard, D.J.E.~~	+	===Crystal Structure of the apo form of Human H-Ferritin variant MIC1===

-	~~Description: Crystal~~ Structure ~~of the apo form of Human H~~-~~Ferritin variant MIC1~~	+
		+	==About this Structure==
		+	[[4dyz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DYZ OCA].
		+	[[Category: Ferroxidase]]
		+	[[Category: Homo sapiens]]
		+	[[Category: Huard, D J.E.]]
		+	[[Category: Tezcan, F A.]]
		+	[[Category: Four-helix bundle]]
		+	[[Category: Oxidoreductase]]

OCA at 07:21, 28 March 2012

OCA — Wed, 28 Mar 2012 07:21:16 GMT

←Older revision		Revision as of 07:21, 28 March 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4dyz is ON HOLD	+	The entry 4dyz is ON HOLD until Paper Publication

	Authors: Tezcan, F.A., Huard, D.J.E.		Authors: Tezcan, F.A., Huard, D.J.E.

	Description: Crystal Structure of the apo form of Human H-Ferritin variant MIC1		Description: Crystal Structure of the apo form of Human H-Ferritin variant MIC1

OCA: Protected "4dyz" [edit=sysop:move=sysop]

OCA — Thu, 08 Mar 2012 05:30:22 GMT

Protected "4dyz" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:30, 8 March 2012

OCA: New page: '''Unreleased structure''' The entry 4dyz is ON HOLD Authors: Tezcan, F.A., Huard, D.J.E. Description: Crystal Structure of the apo form of Human H-Ferritin variant MIC1

OCA — Thu, 08 Mar 2012 05:30:21 GMT

New page: '''Unreleased structure''' The entry 4dyz is ON HOLD Authors: Tezcan, F.A., Huard, D.J.E. Description: Crystal Structure of the apo form of Human H-Ferritin variant MIC1

New page

'''Unreleased structure'''

The entry 4dyz is ON HOLD

Authors: Tezcan, F.A., Huard, D.J.E.

Description: Crystal Structure of the apo form of Human H-Ferritin variant MIC1