Structural Biology - Senior Research Staff - Prof Michael Parker

Prof Michael Parker

Deputy Director
Head, Biota Structural Biology Laboratory, St. Vincent's Institute
Professorial Fellow and Professor, Department of Biochemistry and Molecular Biology and Bio21 Institute, University of Melbourne
National Health & Medical Research Council Senior Principal Research (Honorary) Fellow
Australian Research Council Federation Fellow

Education and Professional Experience

1980            B. Sc. (Hons.), Australian National University
1985            D. Phil., Oxford University, UK
2002-2006   National Health & Medical Research Council Senior Principal Research Fellow
2000-2001   Australian Research Council Professorial Research Fellow
1996-2000   Australian Research Council Senior Research Fellow, St. Vincent's Institute
1991-1996   Welcome Australian Senior Research Fellow, St. Vincent's Institute
1986-1991   Staff Scientist, European Molecular Biology Laboratory, Heidelberg, Germany

Achievements

1999     Gottschalk Medal of the Australian Academy of Science
2001     National Health & Medical Research Council Senior Principal Research Fellowship
2004     GE Healthcare Bio-Sciences Award of the ASBMB
2006     Australian Research Council Federation Fellowship
2010     Fellow of the Australian Academy of Science
2011     Lemberg Medal
2011     Ramaciotti Medal for Excellence in Biomedical Research

Research Interests

Protein crystallography; structure-based drug design; cancer; infection; neurobiology
The Biota Structural Biology Laboratory is focused on three disease areas: cancer, infection (bacterial toxins and viruses) and neurological diseases (Alzheimer's disease, memory loss, epilepsy, anxiety). Our aim is to understand the function of key proteins at a molecular level and to discover small molecules that alter the function of these proteins which may then be developed into clinically useful drugs. The lab uses a wide array of platform technologies including molecular biology, protein chemistry, X-ray crystallography (including the Australian Synchrotron), electrophysiology, virtual screening and structure-based drug design.

Selected Publications

  1. Parker, M.W., Pattus, F., Tucker, A.D. & Tsernoglou, D. (1989) Structure of the membrane-pore-forming fragment of colicin A. Nature 337, 93-96.
  2. Reinemer, P., Dirr, H.W., Ladenstein, R., Huber, R., Lo Bello, M., Federici, G. & Parker, M.W.  (1992) Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8Å resolution. J. Mol. Biol. 227, 214-226.
  3. Parker, M.W., Buckley, J.T., Postma, J.P., Tucker, A.D., Leonard, K., Pattus, F. & Tsernoglou, D. (1994) Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states. Nature 367, 292-295.
  4. Hu, S.H., Parker, M.W., Lei, J.Y., Wilce, M.C., Benian, G.M. & Kemp, B.E.  (1994) Insights into autoregulation from the crystal structure of twitchin kinase. Nature 369, 581-584.
  5. Rossjohn, J., Feil, S.C., McKinstry, W.J., Tweten, R.K. & Parker, M.W. (1997) Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form. Cell 89, 685-692.
  6. Rossjohn, J., Cappai, R., Feil, S.C., Henry, A., McKinstry, W.J., Galatis, D., Hesse, L., Multhaup, G., Beyreuther, K., Masters, C.L. & Parker, M.W. (1999) Crystal structure of the N-terminal, growth factor-like domain of Alzheimer's amyloid precursor protein. Nature Struct. Biol. 6, 327-331.
  7. Barnham, K.J., McKinstry, W.J., Multhaup, G., Galatis, D., Morton, C.J., Curtain, C.C., Williamson, N.A., White, A.R., Hinds, M.G., Norton, R.S., Beyreuther, K., Masters, C.L., Parker, M.W. & Cappai, R. (2003) Structure of the Alzheimer’s disease amyloid precursor protein copper binding domain. A regulator of neuronal copper homeostasis. J. Biol. Chem. 278, 17401-17407.
  8. Brown, R.J., Adams, J.J., Pelekanos, R.A., Wan Y., McKinstry, W.J., Palethorpe, K., Seeber, R.M., Monks, T.A., Eidne, K.A., Parker, M.W. & Waters, M.J. (2005) Model for growth hormone receptor activation based on subunit rotation within a receptor dimer. Nature Struct. Mol. Biol.  12, 814-821.
  9. Albiston, A.L., Morton, C.J., Ng, H.L., Pham, V., Yeatman, H.R., Ye, S., Fernando, R.N., De Bundel, D., Ascher, D.B., Mendelsohn, F.A.O., Parker, M.W. & Chai, S.Y. (2008) Identification and characterization of a new cognitive enhancer based on inhibition of insulin-regulated aminopeptidase. FASEB J. 12, 4209-4217.
  10. Hansen, G., Hercus, T.R., McClure, B.J., Stomski, F.C., Dottore, M., Powell, J., Ramshaw, H., Woodcock, J.M., Xu, Y., Guthridge, M., McKinstry, W.J., Lopez, A.F. & Parker, M.W. (2008) The structure of the GM-CSF receptor complex reveals a distinct mode of cytokine receptor activation. Cell 134, 496-507.