4fvg

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==SPFH domain of mouse stomatin (Crystal form 3)==
==SPFH domain of mouse stomatin (Crystal form 3)==
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<StructureSection load='4fvg' size='340' side='right' caption='[[4fvg]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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<StructureSection load='4fvg' size='340' side='right'caption='[[4fvg]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4fvg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FVG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FVG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4fvg]] 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=4FVG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FVG 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></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fvf|4fvf]], [[4fvj|4fvj]]</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></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Epb7.2, Epb72, Stom ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fvg OCA], [https://pdbe.org/4fvg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fvg RCSB], [https://www.ebi.ac.uk/pdbsum/4fvg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fvg ProSAT]</span></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=4fvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fvg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fvg RCSB], [http://www.ebi.ac.uk/pdbsum/4fvg PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/STOM_MOUSE STOM_MOUSE] Regulates ion channel activity and transmembrane ion transport. Regulates ASIC2 and ASIC3 channel activity.<ref>PMID:15471860</ref> <ref>PMID:22850675</ref>
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Stomatin proteins oligomerize at membranes and have been implicated in ion channel regulation and membrane trafficking. To obtain mechanistic insights into their function, we determined three crystal structures of the conserved stomatin domain of mouse stomatin that assembles into a banana-shaped dimer. We show that dimerization is crucial for the repression of acid-sensing ion channel 3 (ASIC3) activity. A hydrophobic pocket at the inside of the concave surface is open in the presence of an internal peptide ligand and closes in the absence of this ligand, and we demonstrate a function of this pocket in the inhibition of ASIC3 activity. In one crystal form, stomatin assembles via two conserved surfaces into a cylindrical oligomer, and these oligomerization surfaces are also essential for the inhibition of ASIC3-mediated currents. The assembly mode of stomatin uncovered in this study might serve as a model to understand oligomerization processes of related membrane-remodelling proteins, such as flotillin and prohibitin.
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A stomatin dimer modulates the activity of acid-sensing ion channels.,Brand J, Smith ES, Schwefel D, Lapatsina L, Poole K, Omerbasic D, Kozlenkov A, Behlke J, Lewin GR, Daumke O EMBO J. 2012 Jul 31. doi: 10.1038/emboj.2012.203. PMID:22850675<ref>PMID:22850675</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Brand, J]]
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[[Category: Brand J]]
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[[Category: Daumke, O]]
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[[Category: Daumke O]]
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[[Category: Schwefel, D]]
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[[Category: Schwefel D]]
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[[Category: Membrane protein]]
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[[Category: Membrane scaffold]]
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[[Category: Mixed alpha-beta fold]]
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Current revision

SPFH domain of mouse stomatin (Crystal form 3)

PDB ID 4fvg

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