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| | ==Refined solution structure of Schizosaccharomyces pombe Sin1 CRIM domain== | | ==Refined solution structure of Schizosaccharomyces pombe Sin1 CRIM domain== |
| - | <StructureSection load='2rvk' size='340' side='right'caption='[[2rvk]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='2rvk' size='340' side='right'caption='[[2rvk]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2rvk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fission_yeast Fission yeast]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RVK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RVK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2rvk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RVK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RVK FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ruj|2ruj]]</div></td></tr> | + | </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=2rvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rvk OCA], [https://pdbe.org/2rvk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rvk RCSB], [https://www.ebi.ac.uk/pdbsum/2rvk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rvk ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sin1, SPAPYUG7.02c ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</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=2rvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rvk OCA], [https://pdbe.org/2rvk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rvk RCSB], [https://www.ebi.ac.uk/pdbsum/2rvk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rvk ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/SIN1_SCHPO SIN1_SCHPO]] Interacts with the sty1 MAP kinase and has a role in the timing of the initiation of mitosis.<ref>PMID:10428959</ref>
| + | [https://www.uniprot.org/uniprot/SIN1_SCHPO SIN1_SCHPO] Interacts with the sty1 MAP kinase and has a role in the timing of the initiation of mitosis.<ref>PMID:10428959</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: Fission yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Furuita, K]] | + | [[Category: Schizosaccharomyces pombe 972h-]] |
| - | [[Category: Kataoka, S]] | + | [[Category: Furuita K]] |
| - | [[Category: Kojima, C]] | + | [[Category: Kataoka S]] |
| - | [[Category: Shiozaki, K]] | + | [[Category: Kojima C]] |
| - | [[Category: Cell cycle]]
| + | [[Category: Shiozaki K]] |
| - | [[Category: Crim domain]]
| + | |
| - | [[Category: Paramagnetic relaxation enhancement]]
| + | |
| - | [[Category: Sin1]]
| + | |
| - | [[Category: Torc2]]
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| Structural highlights
Function
SIN1_SCHPO Interacts with the sty1 MAP kinase and has a role in the timing of the initiation of mitosis.[1]
Publication Abstract from PubMed
The target of rapamycin (TOR) protein kinase forms multi-subunit TOR complex 1 (TORC1) and TOR complex 2 (TORC2), which exhibit distinct substrate specificities. Sin1 is one of the TORC2-specific subunit essential for phosphorylation and activation of certain AGC-family kinases. Here, we show that Sin1 is dispensable for the catalytic activity of TORC2, but its conserved region in the middle (Sin1CRIM) forms a discrete domain that specifically binds the TORC2 substrate kinases. Sin1CRIM fused to a different TORC2 subunit can recruit the TORC2 substrate Gad8 for phosphorylation even in the sin1 null mutant of fission yeast. The solution structure of Sin1CRIM shows a ubiquitin-like fold with a characteristic acidic loop, which is essential for interaction with the TORC2 substrates. The specific substrate-recognition function is conserved in human Sin1CRIM, which may represent a potential target for novel anticancer drugs that prevent activation of the mTORC2 substrates such as AKT.
Substrate specificity of TOR complex 2 is determined by a ubiquitin-fold domain of the Sin1 subunit.,Tatebe H, Murayama S, Yonekura T, Hatano T, Richter D, Furuya T, Kataoka S, Furuita K, Kojima C, Shiozaki K Elife. 2017 Mar 7;6. pii: e19594. doi: 10.7554/eLife.19594. PMID:28264193[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wilkinson MG, Pino TS, Tournier S, Buck V, Martin H, Christiansen J, Wilkinson DG, Millar JB. Sin1: an evolutionarily conserved component of the eukaryotic SAPK pathway. EMBO J. 1999 Aug 2;18(15):4210-21. PMID:10428959 doi:http://dx.doi.org/10.1093/emboj/18.15.4210
- ↑ Tatebe H, Murayama S, Yonekura T, Hatano T, Richter D, Furuya T, Kataoka S, Furuita K, Kojima C, Shiozaki K. Substrate specificity of TOR complex 2 is determined by a ubiquitin-fold domain of the Sin1 subunit. Elife. 2017 Mar 7;6. pii: e19594. doi: 10.7554/eLife.19594. PMID:28264193 doi:http://dx.doi.org/10.7554/eLife.19594
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