Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1
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.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
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Crystal structure of human uracil-DNA glycosylase in complex with a protein inhibitor: protein mimicry of DNA
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.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis
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.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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