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2rvk
From Proteopedia
(Difference between revisions)
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<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]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2rvk]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RVK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2rvk]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RVK FirstGlance]. <br> |
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ruj|2ruj]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ruj|2ruj]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sin1, SPAPYUG7.02c ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rvk OCA], [http://pdbe.org/2rvk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rvk RCSB], [http://www.ebi.ac.uk/pdbsum/2rvk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rvk ProSAT]</span></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=2rvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rvk OCA], [http://pdbe.org/2rvk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rvk RCSB], [http://www.ebi.ac.uk/pdbsum/2rvk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rvk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://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> | [[http://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> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2rvk" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Fission yeast]] | ||
[[Category: Furuita, K]] | [[Category: Furuita, K]] | ||
[[Category: Kataoka, S]] | [[Category: Kataoka, S]] | ||
Revision as of 07:45, 15 November 2017
Refined solution structure of Schizosaccharomyces pombe Sin1 CRIM domain
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