Article Abstract:
Cyclin-dependent kinases (Cdks) play a key role in the regulation of cell cycle progression. These regulatory proteins consist of 34 kDA catalytic subunits that are linked with cyclin-regulatory subunits. Four biochemical mechanisms control Cdk activity, two of which are those that control these proteins' activation and inhibition. A mutational analysis of the crystal structure of human Cdk2 kinase complex sheds some light on the action of these biochemical mechanisms. Results show that all four beta strands are bound to the kinase C-terminal lobe by CksHs1.
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Article Abstract:
Structural analysis of the uracil-DNA glycosylase inhibitor (Ugi) complexed to human uracil-DNA glycosylase (UDG) shows that 1.9 angstroms Ugi functions as a DNA mimic and provides a structural basis for the binding of UDG to DNA and a crystallographic basis for the design of new DNA repair inhibitors. Ugi, a B. subtilis bacteriophage protein, binds the sequence-conserved DNA-binding groove of UDG through various mechanisms.
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Article Abstract:
The atomic structure of the DNA repair enzyme human uracil-DNA glycosylase (UDG) has been resolved to 2.0 angstroms, and the structure of a UDG-inhibitor complex with 6-aminouracil to 2.3 angstroms. Analysis of human UDG mutant enzymes indicates that the glycosylic bond cleavage involves Gln-144, Asp-145 and His-268. An active-site groove binds extrahelical uracil to remove it from DNA.
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