The solution struture of the reduced yeast TOR1 FATC domain bound to DPC micelles at 298K

lipid-/membrane binding and regulation thereof

the redox-state of the FATC influences the cellular stability of TOR

same protein in the free, oxidized state at 298K

same protein in the oxidized from bound to DPC micelles at 318K

Structural basis for the association of the redox-sensitive target of rapamycin FATC domain with membrane-mimetic micelles.

The Solution Structure Of The Fatc Domain Of The Protein Kinase Tor1 From Yeast

Nmr Structure Of The Oxidized Yeast Tor1 Fatc Domain Bound To Dpc Micelles At 318k

K7_Tor1p [Saccharomyces cerevisiae Kyokai no. 7]

mutant drr1-1 protein [Saccharomyces cerevisiae]

Tor1p [Saccharomyces cerevisiae YJM1078]

phosphatidylinositol kinase-related protein kinase TOR1 [Saccharomyces cerevisiae S288c]

RecName: Full=Serine/threonine-protein kinase TOR1; AltName: Full=Dominant rapamycin resistance protein 1; AltName: Full=Phosph

TPA: phosphatidylinositol kinase-related protein kinase TOR1 [Saccharomyces cerevisiae S288c]

pGEV2 ref.:
JR Huth et al., Protein Sci. 6:2359-2364, 1997

Dames group, Biozentrum, University of Basel

torsion angle dynamics, simulated annealing

oxidized yeast TOR1 FATC domain bound to DPC micelles, 318K

oxidized yeast TOR1 FATC domain in solution, 298K

50 mM Tris, 100 mM NaCl, 20 mM TCEP, 170 mM dodecylphophocholine (DPC)

Institut de Biologie Structurale J.P. EBEL CEA-CNRS, Grenoble, France

Schwieters, Kuszewski, Tjandra and Clore

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax