5FLC

Architecture of human mTOR Complex 1 - 5.9 Angstrom reconstruction

5FLC の概要

• エントリーDOI: 10.2210/pdb5flc/pdb
• EMDBエントリー: 3213
• 分子名称: SERINE/THREONINE-PROTEIN KINASE MTOR, REGULATORY-ASSOCIATED PROTEIN OF MTOR, FKBP, ... (7 entities in total)
• 機能のキーワード: transferase, rapamycin, mtorc1
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 702027.97

構造登録者

Aylett, C.H.S.,Sauer, E.,Imseng, S.,Boehringer, D.,Hall, M.N.,Ban, N.,Maier, T. (登録日: 2015-10-23, 公開日: 2015-12-30, 最終更新日: 2024-05-08)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (5.9 Å)