
Crystal structures show the binding of a series of anti-malarial compounds to the co-factor binding groove of Plasmodium falciparum lactate dehydrogenase, an essential glycolytic enzyme for the parasite.
Biomolecular Structures
The vast majority of life processes result from the binding of a protein to another molecule. Understanding these interactions at the molecular level is the key to life itself, and provides invaluable insight for the treatment of diseases.
Through the study of protein structure, primarily using protein crystallography, we aim to probe crucial biomolecular interactions central to a variety of diseases. The aim is very much to use this information to accelerate the development of new drugs and therapeutics.
Studies within the group focus on a variety of proteins including immune system proteins, nerve growth factor receptors, transcription factors, plant cell-signalling proteins and metabolic enzymes involved in both malaria and Alzheimer's Disease. We employ a wide range of techniques from recombinant DNA technology, protein purification and characterisation, proteomics approaches through to structure determination using crystallography and molecular modelling.
Michael Booth, Nick Burton, Apirat Chaikaud, Rebecca Conners, Victoria Fairweather and Tim Joseph-Horne.
Ahn, J.H., Miller, D., Winter, V.J., Banfield, M.J., Lee, J.H., Soo, S.Y., Henz, S.R., Brady, R.L., and Weigel, D. (2006) A divergent external loop confers antagonistic activity on floral regulators FT and TFL1. EMBO Journal 25 605-614.
Conners, R., Hooley, E., Clarke, A.R., Thomas, S. and Brady, R.L. (2006) Recognition of oxidatively modified bases within the biotin binding site of avidin. Journal of Molecular Biology 357 263-274.
Booth MPS, Conners R, Rumsby G & Brady RL (2006) Structural basis of substrate specificity in human glyoxylate reductase/hydroxypyruvate reductase Journal of Molecular Biology 360, 1, 178-189
Uhlemann A, Cameron A, Eckstein-Ludwig U, Fischbarg J, Iserovich P, Zuniga F, East M, Lee A, Brady L, Haynes R & Krishna S (2005) A single amino acid residue can determine the sensitivity of SERCAs to artemisinins Nature Structural & Molecular Biology 12, 628 - 629