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	Mol. Cell Aug (2007); 27(3):509-16
Structure of TOR and Its Complex with KOG1-
Adami A, Garcia-Alvarez B, Arias-Palomo E, Barford D, Llorca O
Section of Structural Biology, Chester Beatty Laboratories, Institute of Cancer Research, 237 Fulham Road, London SW3 6JB, UK-
Abstract: The target of rapamycin -TOR- is a large -281 kDa- conserved Ser-Thr protein kinase that functions as a central controller of cell growth- TOR assembles into two distinct multiprotein complexes- TORC1 and TORC2- A defining feature of TORC1 is the interaction of TOR with KOG1 -Raptor in mammals- and its sensitivity to a rapamycin-FKBP12 complex- Here, we have reconstructed in three dimensions the 25 A resolution structures of endogenous budding yeast TOR1 and a TOR-KOG1 complex, using electron microscopy- TOR features distinctive N-terminal HEAT repeats that form a curved tubular-shaped domain that associates with the C-terminal WD40 repeat domain of KOG1- The N terminus of KOG1 is in proximity to the TOR kinase domain, likely functioning to bring substrates into the vicinity of the catalytic region- A model is proposed for the molecular architecture of the TOR-KOG1 complex explaining its sensitivity to rapamycin-
[PUBMED: 17679098]