3f32: Difference between revisions

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[[Image:3f32.png|left|200px]]


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==Horse spleen apoferritin==
The line below this paragraph, containing "STRUCTURE_3f32", creates the "Structure Box" on the page.
<StructureSection load='3f32' size='340' side='right'caption='[[3f32]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3f32]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F32 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<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>
{{STRUCTURE_3f32|  PDB=3f32  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3f32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f32 OCA], [https://pdbe.org/3f32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f32 RCSB], [https://www.ebi.ac.uk/pdbsum/3f32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f32 ProSAT]</span></td></tr>
</table>
== Function ==
[https://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).
== 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/f3/3f32_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=3f32 ConSurf].
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== Publication Abstract from PubMed ==
Propofol is the most widely used injectable general anesthetic. Its targets include ligand-gated ion channels such as the GABA(A) receptor, but such receptor-channel complexes remain challenging to study at atomic resolution. Until structural biology methods advance to the point of being able to deal with systems such as the GABA(A) receptor, it will be necessary to use more tractable surrogates to probe the molecular details of anesthetic recognition. We have previously shown that recognition of inhalational general anesthetics by the model protein apoferritin closely mirrors recognition by more complex and clinically relevant protein targets; here we show that apoferritin also binds propofol and related GABAergic anesthetics, and that the same binding site mediates recognition of both inhalational and injectable anesthetics. Apoferritin binding affinities for a series of propofol analogs were found to be strongly correlated with the ability to potentiate GABA responses at GABA(A) receptors, validating this model system for injectable anesthetics. High resolution x-ray crystal structures reveal that, despite the presence of hydrogen bond donors and acceptors, anesthetic recognition is mediated largely by van der Waals forces and the hydrophobic effect. Molecular dynamics simulations indicate that the ligands undergo considerable fluctuations about their equilibrium positions. Finally, apoferritin displays both structural and dynamic responses to anesthetic binding, which may mimic changes elicited by anesthetics in physiologic targets like ion channels.


===Horse spleen apoferritin===
A unitary anesthetic binding site at high resolution.,Vedula LS, Brannigan G, Economou NJ, Xi J, Hall MA, Liu R, Rossi MJ, Dailey WP, Grasty KC, Klein ML, Eckenhoff RG, Loll PJ J Biol Chem. 2009 Sep 4;284(36):24176-84. Epub 2009 Jul 15. PMID:19605349<ref>PMID:19605349</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3f32" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_19605349}}, adds the Publication Abstract to the page
*[[Ferritin 3D structures|Ferritin 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 19605349 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_19605349}}
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</StructureSection>
==About this Structure==
3F32 is a 1 chain structure of 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=3F32 OCA].
 
==Reference==
<ref group="xtra">PMID:19605349</ref><references group="xtra"/>
[[Category: Equus caballus]]
[[Category: Equus caballus]]
[[Category: Eckenhoff, R G.]]
[[Category: Large Structures]]
[[Category: Economou, N J.]]
[[Category: Eckenhoff RG]]
[[Category: Loll, P J.]]
[[Category: Economou NJ]]
[[Category: Rossi, M J.]]
[[Category: Loll PJ]]
[[Category: Vedula, L S.]]
[[Category: Rossi MJ]]
[[Category: 4-helix bundle]]
[[Category: Vedula LS]]
[[Category: Acetylation]]
[[Category: Iron]]
[[Category: Iron storage]]
[[Category: Metal binding protein]]
[[Category: Metal-binding]]
 
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