5FLC

Architecture of human mTOR Complex 1 - 5.9 Angstrom reconstruction

Summary for 5FLC

• Entry DOI: 10.2210/pdb5flc/pdb
• EMDB information: 3213
• Descriptor: SERINE/THREONINE-PROTEIN KINASE MTOR, REGULATORY-ASSOCIATED PROTEIN OF MTOR, FKBP, ... (7 entities in total)
• Functional Keywords: transferase, rapamycin, mtorc1
• Biological source: HOMO SAPIENS (HUMAN); More
• Total number of polymer chains: 12
• Total formula weight: 702027.97

Authors

Aylett, C.H.S.,Sauer, E.,Imseng, S.,Boehringer, D.,Hall, M.N.,Ban, N.,Maier, T. (deposition date: 2015-10-23, release date: 2015-12-30, Last modification date: 2024-05-08)

Primary citation

Aylett, C.H.S.,Sauer, E.,Imseng, S.,Boehringer, D.,Hall, M.N.,Ban, N.,Maier, T.
Architecture of Human Mtor Complex 1
Science, 351:48-, 2016

PubMed Abstract: 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.

PubMed: 26678875
DOI: 10.1126/SCIENCE.AAA3870

Experimental method

ELECTRON MICROSCOPY (5.9 Å)