Crystal structure of the p27(sup Kip1) cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex
Article Abstract:
The human p27(sup Kip1) kinase inhibitory domain binds to the phosphorylated cyclin A-cyclin dependent kinase 2(Cdk2) complex as an extended structure which associates with both subunits. The major hydrophobic and hydrogen-bond interactions between 10-amino-acid area of p27 and a shallow groove of cyclin A aid the initial binding and the subsequent associations with Cdk2. The catalytic activity of CDK is suppressed by p27 binding due to its associations with N-terminal beta-sheet of the Cdk2. It also fills up the catalytic cleft, which removes all possibility of ATP binding.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
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Structure of the retinoblastoma tumour-suppressor pocket domain bound to a peptide from HPV E7
Article Abstract:
The pocket domain of the retinoblastoma (Rb) tumour suppressor is involved in Rb function and is often inactivated by the binding of the human papilloma virus E7 oncoprotein in cervical cancer. The crystal structure of the Rb pocket bound to an HPv-16 E7 LxCxE peptide is described, and the implications of the structure in understanding the protein-binding activity of Rb, its regulation and inactivation in cancer, are discussed.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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