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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
PubMed

Insights

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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