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1h96
From Proteopedia
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| - | [[Image:1h96.gif|left|200px]]<br /><applet load="1h96" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1h96, resolution 1.60Å" /> | ||
| - | '''RECOMBINANT MOUSE L-CHAIN FERRITIN'''<br /> | ||
| - | == | + | ==recombinant mouse L-chain ferritin== |
| + | <StructureSection load='1h96' size='340' side='right'caption='[[1h96]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1h96]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H96 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H96 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1h96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h96 OCA], [https://pdbe.org/1h96 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h96 RCSB], [https://www.ebi.ac.uk/pdbsum/1h96 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h96 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FRIL1_MOUSE FRIL1_MOUSE] 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. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h9/1h96_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1h96 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Cubic F432 crystals of recombinant mouse L-chain apoferritin were obtained by the hanging-drop technique with ammonium sulfate and cadmium sulfate as precipitants. The structure was refined to 2.1 and 1.6 A resolution from data obtained at room temperature and under cryogenic conditions, respectively. The structure of an eight-amino-acid loop insertion in the mouse sequence is found to be highly disordered both at room temperature and at low temperature. | Cubic F432 crystals of recombinant mouse L-chain apoferritin were obtained by the hanging-drop technique with ammonium sulfate and cadmium sulfate as precipitants. The structure was refined to 2.1 and 1.6 A resolution from data obtained at room temperature and under cryogenic conditions, respectively. The structure of an eight-amino-acid loop insertion in the mouse sequence is found to be highly disordered both at room temperature and at low temperature. | ||
| - | + | Structure of mouse L-chain ferritin at 1.6 A resolution.,Granier T, Gallois B, Langlois d'Estaintot B, Dautant A, Chevalier JM, Mellado JM, Beaumont C, Santambrogio P, Arosio P, Precigoux G Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1491-7. Epub 2001, Oct 25. PMID:11679711<ref>PMID:11679711</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1h96" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Ferritin 3D structures|Ferritin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Arosio P]] | ||
| + | [[Category: Beaumont C]] | ||
| + | [[Category: Chevalier JM]] | ||
| + | [[Category: D'Estaintot BL]] | ||
| + | [[Category: Dautant A]] | ||
| + | [[Category: Gallois B]] | ||
| + | [[Category: Granier T]] | ||
| + | [[Category: Mellado JM]] | ||
| + | [[Category: Precigoux G]] | ||
| + | [[Category: Santambrogio P]] | ||
Current revision
recombinant mouse L-chain ferritin
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