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Laboratory of Molecular Biophysics
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Our major interests are in the biochemical and structural basis of molecular interactions that underlie cytoplasmic signal transduction. Almost all cellular processes are controlled by phosphorylation catalysed by protein kinases. Studies on the 27 or so protein kinase structures that have been solved to date show that they all have a common core structure but each has a distinct substrate specificity and a distinct mechanism for control. The importance of phospho-signalling pathways in eukaryotic signal transduction is demonstrated by the observation that the human genome contains 575 protein kinases, the third most populous domain in the entire proteome. We employ X-ray crystallographic methods and more recently electron microscopy (see also Section 11.2 by Dr Catherine Vénien-Bryan). Much effort is required on expression and purification methods to provide suitable quantities of proteins. We address the following themes: How is specificity achieved in molecular recognition? How do regulatory subunits exert their control? What is the structural basis for the catalytic mechanism? How can knowledge of structure be exploited in understanding drug interactions?
Cell cycle proteins: studies with CDK2 |
Regulation of Phosphorylase KinaseAtlanta Cook and Ed Lowe |
Protein interactions in Protein KinasesA. Cook and J. Gruber |
CDK Activating Kinase (CAK)Nick R. Brown and John Sinclair |
Polo-like kinase (Plk1)John Sinclair and Hawei Song in collaboration with Erich A. Nigg (Max Planck Institute for Biochemistry, Martinsried) |
Electron microscopy of DNA scaffoldsJ. Robin Harris in collaboration with James Mitchell and Andrew Turberfield, Department of Physics, University of Oxford |
Acknowledgments and References |
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