2rvk
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Refined solution structure of Schizosaccharomyces pombe Sin1 CRIM domain== | |
| + | <StructureSection load='2rvk' size='340' side='right'caption='[[2rvk]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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='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> | ||
| + | == 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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:28264193</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 2rvk" style="background-color:#fffaf0;"></div> |
| - | [[Category: Furuita | + | == References == |
| - | [[Category: Kojima | + | <references/> |
| - | [[Category: Shiozaki | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Schizosaccharomyces pombe 972h-]] | ||
| + | [[Category: Furuita K]] | ||
| + | [[Category: Kataoka S]] | ||
| + | [[Category: Kojima C]] | ||
| + | [[Category: Shiozaki K]] | ||
Current revision
Refined solution structure of Schizosaccharomyces pombe Sin1 CRIM domain
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