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Structure of TOR and its complex with KOG1
Alessandra Adami1, Begoña García-Alvarez, Ernesto Arias-Palomo
1Section of Structural Biology, Chester Beatty Laboratories, Institute of Cancer Research, 237 Fulham Road, London, UK.
Molecular Cell
|August 7, 2007
Summary
The target of rapamycin (TOR) protein complex
Area of Science:
- Molecular Biology
- Cell Biology
- Structural Biology
Background:
- The target of rapamycin (TOR) is a crucial protein kinase regulating cell growth.
- TOR exists in two complexes, TORC1 and TORC2.
- TORC1 interacts with KOG1 (Raptor) and is sensitive to rapamycin.
Purpose of the Study:
- To determine the three-dimensional structure of yeast TOR1 and a TOR-KOG1 complex.
- To elucidate the molecular architecture of the TOR-KOG1 complex.
Main Methods:
- Three-dimensional reconstruction using electron microscopy.
- Analysis of endogenous budding yeast TOR1 and TOR-KOG1 complex at 25 A resolution.
Main Results:
- The structure reveals TOR's N-terminal HEAT repeats forming a curved domain.
- This domain associates with KOG1's C-terminal WD40 repeat domain.
- KOG1's N terminus is near the TOR kinase domain, potentially aiding substrate binding.
Conclusions:
- A structural model for the TOR-KOG1 complex is proposed.
- This model explains the complex's sensitivity to rapamycin.
- Understanding TOR complex structure provides insights into cell growth regulation.
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