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Active and Inactive Protein Kinases: Structural Basis for Regulation
The structural basis for control of eukaryotic protein kinases.
Mechanisms for kinase activation through phosphorylation, additional domains or subunits, by scaffolding proteins and by kinase dimerization are discussed.
The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases
This structure provides an explanation for the specificity of CDK2 towards the proline that follows the phosphorylatable serine of the substrate peptide, and the requirement for the basic residue in the P+3 position of the substrates, HHASPRK.
The structure of P‐TEFb (CDK9/cyclin T1), its complex with flavopiridol and regulation by phosphorylation
The structures of the CDK9/CycT1 and free cyclin T2 are determined to understand the regulation of a transcriptional CDK by its cognate cyclin and shows flexibility that may be important for the interaction of this region with HIV TAT and HEXIM.
Glycogen phosphorylase: control by phosphorylation and allosteric effectors
- L. Johnson
- Biology, ChemistryFASEB journal : official publication of the…
- 1 March 1992
The allosteric mechanism of activation of phosphorylase by phosphorylation may be relevant to other enzymes although it is now known that other mechanisms such as electrostatic steric blocking mechanisms also exist.
Protein Kinase Inhibitors: Insights into Drug Design from Structure
This review focuses on kinase inhibitors that are in the clinic or in clinical trials and for which structural information is available and which have provided insights into targeting the inactive or active form of the kinase, for targeting the global constellation of residues at the ATP site, and into targeting noncatalytic domains.
Effects of Phosphorylation of Threonine 160 on Cyclin-dependent Kinase 2 Structure and Activity*
Phosphorylated cyclin-dependent protein kinase 2 (CDK2) is prepared for crystallization using the CDK-activating kinase 1 (CAK1) from Saccharomyces cerevisiae and grown crystals using microseeding techniques.
The crystal structure of human CDK7 and its protein recognition properties.
Structural basis for control by phosphorylation.
The recently solved structure of the active phosphorylase kinase catalytic domain in complex with a peptide substrate demonstrates a key role for the activation segment in substrate recognition that is likely to be common for many protein kinases.