title: Structural basis for activation of the autoinhibitory C-terminal kinase domain of p90 RSK2.
abstract: 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.
authors: The Hormel Institute, University of Minnesota, 801 16th Avenue NE, Austin, Minnesota 55912, USA.
authors: Margarita
authors: M
authors: Malakhova
authors: Valentina
authors: V
authors: Tereshko
authors: Sung-Young
authors: SY
authors: Lee
authors: Ke
authors: K
authors: Yao
authors: Yong-Yeon
authors: YY
authors: Cho
authors: Ann
authors: A
authors: Bode
authors: Zigang
authors: Z
authors: Dong
mesh_terms: 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*
chemical_list: D038744:Ribosomal Protein S6 Kinases, 90-kDa; C069330:ribosomal protein S6 kinase, 90kDa, polypeptide 3