Odell, Mark - University of Westminster - Department of Life Sciences

个人简介

Dr Mark Odell studies the structure and function of proteins through protein biochemistry, crystallography allied with rational mutagenesis and bioinformatics. Dr Odell studied for his doctorate under Professor Geoffrey Smith (Imperial) in Oxford where he characterised the biochemistry of the Vaccinia virus DNA ligase enzyme and learnt protein purification with Professor Dale Wigley (ICRF, UK). Dr Odell then moved to The Sloan-Kettering Institute in New York to study with Professor Stewart Shuman. His work there culminated in a model for the process of DNA recognition by all eukaryotic DNA ligases built on a novel ligase-adenylate crystal structure supported by site directed mutagenesis Odell et al(2000) Molecular Cell 6, 1183-1193. Dr Odell gained experience of protein biochemistry and mutagenesis with Professor Shuman and protein crystallisation, diffraction data collection and data processing with Professor Dimitar Nikolov. Dr Odell completed a second post-doctoral appointment at the Department of Genetics, Leicester, under Professor Bambos Kyriacou where he studied proteins that form the molecular basis for the circadian clock in Drosophila. In Leicester he worked on recombinant circadian protein expression and gained experience in protein analysis by bioinformatics and two-dimensional protein electrophoresis. Since establishing his research group in his first appointment Dr Odell continues to study DNA ligase biology but has now sought new avenues of research into protein structure and function in collaboration with various colleagues Dr Miriam Dwek (Biosciences, Westminster), Dr Peter Moody (Biochemistry, Leicester), Professor Igor Barsukov (Liverpool), Professor Greg Blatch (Rhodes University, South Africa) and Dr Steve Smerdon (NIMR, Mill Hill).

研究领域

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Dr Odell's laboratory is focussing on the insight that protein structure can bring to problems in molecular biology, particularly in disease states. They are using a combination of biochemistry, molecular biology and biophysics to illuminate protein chemistry and molecular interactions. DNA ligase biology is a key component of the work in his group. The Paramecium bursaria Chlorella virus 1 (PBCV-1) DNA ligase is a paradigm for the transitions in all ATP-dependent DNA ligase enzymes that accompany their various catalytic steps. In a collaborative venture with Peter Moody (Leicester, Biochemistry) and Igor Barsukov (Liverpool) they are studying the recognition of DNA by the minimalist PBCV-1 enzyme and the more complex cellular human DNA ligase I. Using insights gained from a multi-disciplinary approach (crystallography, NMR, biochemistry and surface plasmon resonance) they are building a dynamic picture of the binding of ATP-dependent DNA ligases to DNA. This is a more complete picture of the structural rearrangements that accompany DNA ligases during their catalytic cycle than can be appreciated from a single static crystal structure. The laboratory is also investigating DNA ligase enzymes from a number of pathogenic sources, including Campyllobacter jejunii and Trichomonas vaginalis, for their function and biochemistry.