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2rvk

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Current revision

Refined solution structure of Schizosaccharomyces pombe Sin1 CRIM domain

Structural highlights

2rvk is a 1 chain structure with sequence from Schizosaccharomyces pombe 972h-. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2rvk"

@@ Line 1: / Line 1: @@
 ==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 ==
-<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>
-<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>
+[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 ==
@@ Line 23: / Line 21: @@
 __TOC__
 </StructureSection>
-[[Category: Fission yeast]]
 [[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]]

2rvk

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Current revision

Refined solution structure of Schizosaccharomyces pombe Sin1 CRIM domain

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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