Article
Structural diversity of the active N-terminal kinase domain of p90 ribosomal S6 kinase 2.
PloS one - 30 Nov 2009
Malakhova Margarita, Kurinov Igor, Liu Kangdong, Zheng Duo, D'Angelo Igor, Shim Jung-Hyun, Steinman Valerie, Bode Ann M, Dong Zigang
Abstract excerpt
The p90 ribosomal protein kinase 2 (RSK2) is a highly expressed Ser/Thr kinase activated by growth factors and is involved in cancer cell proliferation and tumor promoter-induced cell transformation. RSK2 possesses two non-identical kinase domains, and the structure of its N-terminal domain (NTD), which is responsible for phosphorylation of a variety of substrates, is unknown. The crystal structure of the NTD...
Topics
- Adenosine Triphosphate
- Animals
- Binding Sites
- Crystallography, X-Ray
- Escherichia coli
- Glutamic Acid
- Lysine
- Mice
- Molecular Conformation
- Mutation
- Phosphorylation