Structural basis for activation of the autoinhibitory C-terminal kinase domain of p90 RSK2.
The X-ray structure at 2.0-A resolution of the p90 ribosomal S6 kinase 2 C-terminal kinase domain revealed a C-terminal autoinhibitory alphaL-helix that was embedded in the kinase scaffold and determines the inactive kinase conformation. We suggest a mechanism of activation through displacement of the alphaL-helix and rearrangement of the conserved residue Glu500, as well as the reorganization of the T-loop into the active conformation.
Malakhova
Margarita
M
The Hormel Institute, University of Minnesota, 801 16th Avenue NE, Austin, Minnesota 55912, USA.
Tereshko
Valentina
V
Lee
Sung-Young
SY
Yao
Ke
K
Cho
Yong-Yeon
YY
Bode
Ann
A
Dong
Zigang
Z
D018360:Crystallography, X-Ray; D004789:Enzyme Activation; D008958:Models, Molecular; D011487:Protein Conformation; D038744:Ribosomal Protein S6 Kinases, 90-kDa / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*
D038744:Ribosomal Protein S6 Kinases, 90-kDa; C069330:ribosomal protein S6 kinase, 90kDa, polypeptide 3