4fvf | pdb_00004fvf

SPFH domain of mouse stomatin (Crystal form 1)

spinqualitylabelsall models 4fvf, resolution 2.46Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4fvf is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, CD Related: 4fvj, 4fvg Gene: Epb7.2, Epb72, Stom (Mus musculus) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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