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Architecture of human mTOR complex 1

Aylett, Christopher H. S. ; Sauer, Evelyn ; Imseng, Stefan ; Boehringer, Daniel ; Hall, Michael N. ; Ban, Nenad ; Maier, Timm

Science (American Association for the Advancement of Science), 2016-01, Vol.351 (6268), p.48-52 [Periódico revisado por pares]

United States: American Association for the Advancement of Science

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Título:
Architecture of human mTOR complex 1
Autor: Aylett, Christopher H. S. ; Sauer, Evelyn ; Imseng, Stefan ; Boehringer, Daniel ; Hall, Michael N. ; Ban, Nenad ; Maier, Timm
Assuntos: Adaptor Proteins, Signal Transducing - chemistry ; Architecture ; Cancer ; Catalytic Domain ; Cell growth ; Cryoelectron Microscopy ; Diabetes ; Government regulations ; Humans ; Kinases ; Leucine ; Mechanistic Target of Rapamycin Complex 1 ; Mechanistic Target of Rapamycin Complex 2 ; Metabolism ; MTOR Associated Protein, LST8 Homolog ; Multiprotein Complexes - chemistry ; Protein Binding ; Protein Multimerization ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins ; Regulatory-Associated Protein of mTOR ; Substrate Specificity ; Tacrolimus Binding Proteins - chemistry ; TOR Serine-Threonine Kinases - chemistry
É parte de: Science (American Association for the Advancement of Science), 2016-01, Vol.351 (6268), p.48-52
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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Descrição: 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.
Editor: United States: American Association for the Advancement of Science
Idioma: Inglês

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Architecture of human mTOR complex 1

Aylett, Christopher H. S. ; Sauer, Evelyn ; Imseng, Stefan ; Boehringer, Daniel ; Hall, Michael N. ; Ban, Nenad ; Maier, Timm

United States: American Association for the Advancement of Science

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