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| | <StructureSection load='5cuf' size='340' side='right'caption='[[5cuf]], [[Resolution|resolution]] 3.50Å' scene=''> | | <StructureSection load='5cuf' size='340' side='right'caption='[[5cuf]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5cuf]] is a 5 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=5CUF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CUF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5cuf]] is a 5 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=5CUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CUF FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SESN2, SEST2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5cuf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cuf OCA], [https://pdbe.org/5cuf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cuf RCSB], [https://www.ebi.ac.uk/pdbsum/5cuf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cuf ProSAT]</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=5cuf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cuf OCA], [http://pdbe.org/5cuf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cuf RCSB], [http://www.ebi.ac.uk/pdbsum/5cuf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cuf ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SESN2_HUMAN SESN2_HUMAN]] Involved in the reduction of peroxiredoxins.<ref>PMID:15105503</ref> | + | [https://www.uniprot.org/uniprot/SESN2_HUMAN SESN2_HUMAN] Involved in the reduction of peroxiredoxins.<ref>PMID:15105503</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: An, S]] | + | [[Category: An S]] |
| - | [[Category: Cho, U S]] | + | [[Category: Cho U-S]] |
| - | [[Category: Kim, H]] | + | [[Category: Kim H]] |
| - | [[Category: Lee, J H]] | + | [[Category: Lee JH]] |
| - | [[Category: Ro, S H]] | + | [[Category: Ro S-H]] |
| - | [[Category: Alkylhydroperoxidase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
SESN2_HUMAN Involved in the reduction of peroxiredoxins.[1]
Publication Abstract from PubMed
Sestrins are stress-inducible metabolic regulators with two seemingly unrelated but physiologically important functions: reduction of reactive oxygen species (ROS) and inhibition of the mechanistic target of rapamycin complex 1 (mTORC1). How Sestrins fulfil this dual role has remained elusive so far. Here we report the crystal structure of human Sestrin2 (hSesn2), and show that hSesn2 is twofold pseudo-symmetric with two globular subdomains, which are structurally similar but functionally distinct from each other. While the N-terminal domain (Sesn-A) reduces alkylhydroperoxide radicals through its helix-turn-helix oxidoreductase motif, the C-terminal domain (Sesn-C) modified this motif to accommodate physical interaction with GATOR2 and subsequent inhibition of mTORC1. These findings clarify the molecular mechanism of how Sestrins can attenuate degenerative processes such as aging and diabetes by acting as a simultaneous inhibitor of ROS accumulation and mTORC1 activation.
Janus-faced Sestrin2 controls ROS and mTOR signalling through two separate functional domains.,Kim H, An S, Ro SH, Teixeira F, Jin Park G, Kim C, Cho CS, Kim JS, Jakob U, Hee Lee J, Cho US Nat Commun. 2015 Nov 27;6:10025. doi: 10.1038/ncomms10025. PMID:26612684[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Budanov AV, Sablina AA, Feinstein E, Koonin EV, Chumakov PM. Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD. Science. 2004 Apr 23;304(5670):596-600. PMID:15105503 doi:http://dx.doi.org/10.1126/science.1095569
- ↑ Kim H, An S, Ro SH, Teixeira F, Jin Park G, Kim C, Cho CS, Kim JS, Jakob U, Hee Lee J, Cho US. Janus-faced Sestrin2 controls ROS and mTOR signalling through two separate functional domains. Nat Commun. 2015 Nov 27;6:10025. doi: 10.1038/ncomms10025. PMID:26612684 doi:http://dx.doi.org/10.1038/ncomms10025
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