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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.

SUBMITTER: Malakhova M 

PROVIDER: S-EPMC2864125 | biostudies-literature | 2008 Jan

REPOSITORIES: biostudies-literature

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Structural basis for activation of the autoinhibitory C-terminal kinase domain of p90 RSK2.

Malakhova Margarita M   Tereshko Valentina V   Lee Sung-Young SY   Yao Ke K   Cho Yong-Yeon YY   Bode Ann A   Dong Zigang Z  

Nature structural & molecular biology 20071216 1


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. ...[more]

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