Tor forms a dimer through an N-terminal helical solenoid with a complex topology
Abstract
The target of rapamycin (Tor) is a Ser/Thr protein kinase that regulates a range of anabolic and catabolic processes. Tor is present in two complexes, TORC1 and TORC2, in which the Tor-Lst8 heterodimer forms a common sub-complex. We have determined the cryo-electron microscopy (EM) structure of Tor bound to Lst8. Two Tor-Lst8 heterodimers assemble further into a dyad-symmetry dimer mediated by Tor-Tor interactions. The first 1,300 residues of...
Paper Details
Title
Tor forms a dimer through an N-terminal helical solenoid with a complex topology
Published Date
Apr 13, 2016
Journal
Volume
7
Issue
1
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