2rvk: Difference between revisions
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The | ==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]] | |||
Latest revision as of 20:54, 12 April 2023
Refined solution structure of Schizosaccharomyces pombe Sin1 CRIM domain
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