Mark Sanderson

Investigation into the structure and function of DNA-binding proteins and of viral proteins of clinical interest using X-ray crystallography and High field NMR. My research group has solved the structure of the key protein involved in Herpes treatment, namely the thymidine kinase and has solved the complexes of this target with all the clinically administered drugs as well as newly developed compounds using X-ray crystallography. We have solved the X-ray crystal structure of a key family of 2^nd generation antibiotics (the quinolones such as levofloxacin and moxifloxacin) in complex with their target, the type II topoisomerase-DNA-complex. The first complex we solved was with the topoisomerase from Streptococcus pneumoniae. More recently we have solved these complexes from a wide range of topoisomerases from different pathogenic organisms in collaboration with Prof. Mark Fisher’s group at St. George’s. In collaboration with Prof. Michael Malim’s group we have very recently solved the solution structure of the complex of the binding domain of HIV Vif with Elongin B-Elongin C using High field NMR spectra recorded at 700, 800 and 900 MHz. Previously we studied this system using a wide range of biophysical, virological, and molecular biological techniques.

Structure and function of DNA-binding proteins; structural studies of viral proteins.

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