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| | <StructureSection load='5dj4' size='340' side='right'caption='[[5dj4]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='5dj4' size='340' side='right'caption='[[5dj4]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5dj4]] 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=5DJ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DJ4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5dj4]] 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=5DJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DJ4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.697Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene></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=5dj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dj4 OCA], [http://pdbe.org/5dj4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dj4 RCSB], [http://www.ebi.ac.uk/pdbsum/5dj4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dj4 ProSAT]</span></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=5dj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dj4 OCA], [https://pdbe.org/5dj4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dj4 RCSB], [https://www.ebi.ac.uk/pdbsum/5dj4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dj4 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: Knockenhauer, K E]] | + | [[Category: Knockenhauer KE]] |
| - | [[Category: Saxton, R A]] | + | [[Category: Saxton RA]] |
| - | [[Category: Schwartz, T U]] | + | [[Category: Schwartz TU]] |
| - | [[Category: Amino-acid]]
| + | |
| - | [[Category: Leucine]]
| + | |
| - | [[Category: Mtor]]
| + | |
| - | [[Category: Sensing]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
SESN2_HUMAN Involved in the reduction of peroxiredoxins.[1]
Publication Abstract from PubMed
Eukaryotic cells coordinate growth with the availability of nutrients through mTOR complex 1 (mTORC1), a master growth regulator. Leucine is of particular importance and activates mTORC1 via the Rag GTPases and their regulators GATOR1 and GATOR2. Sestrin2 interacts with GATOR2 and is a leucine sensor. We present the 2.7-A crystal structure of Sestrin2 in complex with leucine. Leucine binds through a single pocket that coordinates its charged functional groups and confers specificity for the hydrophobic side chain. A loop encloses leucine and forms a lid-latch mechanism required for binding. A structure-guided mutation in Sestrin2 that decreases its affinity for leucine leads to a concomitant increase in the leucine concentration required for mTORC1 activation in cells. These results provide a structural mechanism of amino acid sensing by the mTORC1 pathway.
Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway.,Saxton RA, Knockenhauer KE, Wolfson RL, Chantranupong L, Pacold ME, Wang T, Schwartz TU, Sabatini DM Science. 2015 Nov 19. pii: aad2087. PMID:26586190[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
- ↑ Saxton RA, Knockenhauer KE, Wolfson RL, Chantranupong L, Pacold ME, Wang T, Schwartz TU, Sabatini DM. Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway. Science. 2015 Nov 19. pii: aad2087. PMID:26586190 doi:http://dx.doi.org/10.1126/science.aad2087
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