5ef5: Difference between revisions
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<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=5ef5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ef5 OCA], [http://pdbe.org/5ef5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ef5 RCSB], [http://www.ebi.ac.uk/pdbsum/5ef5 PDBsum]</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=5ef5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ef5 OCA], [http://pdbe.org/5ef5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ef5 RCSB], [http://www.ebi.ac.uk/pdbsum/5ef5 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Target of rapamycin (TOR), a conserved protein kinase and central controller of cell growth, functions in two structurally and functionally distinct complexes: TORC1 and TORC2. Dysregulation of mammalian TOR (mTOR) signaling is implicated in pathologies that include diabetes, cancer, and neurodegeneration. We resolved the architecture of human mTORC1 (mTOR with subunits Raptor and mLST8) bound to FK506 binding protein (FKBP)-rapamycin, by combining cryo-electron microscopy at 5.9 angstrom resolution with crystallographic studies of Chaetomium thermophilum Raptor at 4.3 angstrom resolution. The structure explains how FKBP-rapamycin and architectural elements of mTORC1 limit access to the recessed active site. Consistent with a role in substrate recognition and delivery, the conserved amino-terminal domain of Raptor is juxtaposed to the kinase active site. | |||
Architecture of human mTOR complex 1.,Aylett CH, Sauer E, Imseng S, Boehringer D, Hall MN, Ban N, Maier T Science. 2016 Jan 1;351(6268):48-52. doi: 10.1126/science.aaa3870. Epub 2015 Dec , 17. PMID:26678875<ref>PMID:26678875</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5ef5" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 15:11, 13 January 2016
Crystal structure of Chaetomium thermophilum RaptorCrystal structure of Chaetomium thermophilum Raptor
Structural highlights
Publication Abstract from PubMedTarget of rapamycin (TOR), a conserved protein kinase and central controller of cell growth, functions in two structurally and functionally distinct complexes: TORC1 and TORC2. Dysregulation of mammalian TOR (mTOR) signaling is implicated in pathologies that include diabetes, cancer, and neurodegeneration. We resolved the architecture of human mTORC1 (mTOR with subunits Raptor and mLST8) bound to FK506 binding protein (FKBP)-rapamycin, by combining cryo-electron microscopy at 5.9 angstrom resolution with crystallographic studies of Chaetomium thermophilum Raptor at 4.3 angstrom resolution. The structure explains how FKBP-rapamycin and architectural elements of mTORC1 limit access to the recessed active site. Consistent with a role in substrate recognition and delivery, the conserved amino-terminal domain of Raptor is juxtaposed to the kinase active site. Architecture of human mTOR complex 1.,Aylett CH, Sauer E, Imseng S, Boehringer D, Hall MN, Ban N, Maier T Science. 2016 Jan 1;351(6268):48-52. doi: 10.1126/science.aaa3870. Epub 2015 Dec , 17. PMID:26678875[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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