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

Journal Article · · Nat. Struct. Mol. Biol.
DOI:https://doi.org/10.1038/nsmb1347· OSTI ID:1006499

The X-ray structure at 2.0-{angstrom} resolution of the p90 ribosomal S6 kinase 2 C-terminal kinase domain revealed a C-terminal autoinhibitory {alpha}L-helix that was embedded in the kinase scaffold and determines the inactive kinase conformation. We suggest a mechanism of activation through displacement of the {alpha}L-helix and rearrangement of the conserved residue Glu500, as well as the reorganization of the T-loop into the active conformation.

Research Organization:
Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
Sponsoring Organization:
USDOE
OSTI ID:
1006499
Journal Information:
Nat. Struct. Mol. Biol., Journal Name: Nat. Struct. Mol. Biol. Journal Issue: (1) ; 01, 2008 Vol. 15; ISSN 1545-9993
Country of Publication:
United States
Language:
ENGLISH