Prof Michael Parker

Research Unit

Structural biology


Head, Structural Biology Unit, SVI
Professorial Fellow and Professor, Department of Biochemistry and Molecular Biology, and Director Bio21 Institute, University of Melbourne
NHMRC Senior Principal Research Fellow

Professional Experience

1980 B. Sc. (Hons.), Australian National University
1985 D. Phil., Oxford University, UK
1986-1991  Staff Scientist, European Molecular Biology Laboratory, Heidelberg, Germany
1991-1996 Welcome Australian Senior Research Fellow, SVI
1996-2000 Australian Research Council Senior Research Fellow, SVI
2000-2001 Australian Research Council Professorial Research Fellow
2002-2006 National Health & Medical Research Council Senior Principal Research Fellow
2007-2011 Australian Research Council Federation Fellow
2012-Present National Health & Medical Research Council Senior Principal Research Fellow
2021- National Health & Medical Research Council Leadership Fellow


1991 Wellcome Trust Senior Research Fellowship
1994 University of Melbourne Selwyn-Smith Medical Research Prize
1996 ASBMB Boehringer-Mannheim Medallist
1997 Australian Research Council Senior Research Fellowship
1999 Gottschalk Medal of the Australian Academy of Science
2001 NHMRC Senior Principal Research Fellowship
2004 GE Healthcare Bio-Sciences Award of the ASBMB
2006 Australian Research Council Federation Fellowship
2006 NHMRC Senior Principal Research Fellowship
2010 Fellow of the Australian Academy of Science
2011 ASBMB Lemberg Medal
2011 NHMRC Senior Principal Research Fellowship
2011 Ramaciotti Medal for Excellence in Biomedical Research
2012 Federation of Asian and Oceanian Biochemists and Molecular Biologists Award for Research Excellence
2014 NHMRC Research Excellence Award for top ranked Program grant application
2015 Fellow of the Australian Academy of Health and Medical Sciences
2016 NHMRC Senior Principal Research Fellowship
2016 Bob Robertson Award of the Australian Society for Biophysics for outstanding contributions to biophysics in Australia and New Zealand
2021 NHMRC Leadership Fellow

Research Interests

Protein crystallography; structure-based drug design; cancer; infection; neurobiology
The Structural Biology Unit is focused on three disease areas: cancer, infection (bacterial toxins, parasites and viruses) and neurological diseases neurodegenerative diseases (including Alzheimer's and Parkinson's diseases, motor neuron disease, multiple sclerosis, chronic fatigue syndrome). 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, protein characterisation tools, X-ray crystallography (including the Australian Synchrotron), cryo electron microscopy, NMR, 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. 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.
  3. 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.
  4. Heierhorst, J., Kobe, B., Feil, S.C., Parker, M.W., Benian, G.M., Weiss, K.R. & Kemp, B.E. (1996) Ca2+/S100 regulation of giant protein kinases. Nature 380, 636-639.
  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. Shatursky, O., Heuck, A.P., Shepard, L.A., Rossjohn, J., Parker, M.W., Johnson, A.E. & Tweten, R.K. (1999) The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for pore-forming toxins. Cell 99, 293-299.
  7. Gilbert, R.J., Jiménez, J.L., Chen, S., Tickle, I.J., Rossjohn, J., Parker, M., Andrew, P.W. & Saibil, H.R. (1999) Two structural transitions in membrane pore formation by pneumolysin, the pore-forming toxin of Streptococcus pneumoniae. Cell 97, 647-655.
  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. 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.
  10. Miles, L.A., Crespi, G.A.N., Doughty. L. & Parker, M.W. (2013) Bapineuzumab captures the N-terminus of the Alzheimer’s disease amyloid-beta peptide in a helical conformation. Sci. Rep. 3, 1302; DOI:10.1038/srep01302.
  11. Bennetts, B. & Parker, M.W. (2013) Molecular determinants of common gating of a CIC chloride channel. Nature Commun. 4, 3507.
  12. Brooks, A.J., Dai, W., O’Mara, M.L., Abankwa, D., Chabra, Y., Pelekanos, R.A., Gardon, O., Tunny, K.A., Blucher, K.M., Morton, C.J., Parker, M.W., Sierecki, E., Gambin, Y., Alexandrov, K., Wilson, I.A., Doxastakis, M., Mark, A.E. & Waters, M.J. (2014) A new cytokine receptor activation paradigm: activation of JAK2 by the Growth Hormone Receptor. A mechanism for activation of JAK2 by the growth hormone receptor. Science, 344, 710, 1249783-1-1249783-12.
  13. Morton, C.J., Nero, T.N., Holien, J.K., Wielens, J. & Parker, M.W. (2014) Oncogenic protein interfaces: small molecules, big challenges. Nature Revs. Cancer, 14, 248-262.
  14. Crespi, G.A.N., Hermans, S.J., Parker, M.W. & Miles, L.A. (2015) Molecular basis for mid-region amyloid-b capture by leading Alzheimer’s disease immunotherapies. Sci. Reps. 5, 9649.
  15. Broughton, S.E., Hercus, T.R., Nero, T.L., Kan, W.L., Barry, E.F., Dottore, M., Cheung Tung Shing, K.S., Morton, C.J., Dhagat, U., Hardy, M.P., Wilson, N.J., Downton, M.T., Schieber, C., Hughes, T.P., Lopez A.F. & Parker, M.W. (2018) A dual role for the N-terminal domain of the IL-3 receptor in cell signalling. Nature Communs. 9, 386.
  16. Baell, J.B., Leaver, D., Cleary, B., Nguyen, N., Natalie L. Downer, L.D., Vanyai, H.K., Bergamasco, M.I., May, R.E., Wang, B., Wilcox, S., Garnham, A., Pacini, G., Zamudio, N., Sheikh, B.N., Doggett, K., Mieruszynski, S., Heath, J.K., Chung, M.C., Hermans, S.J., Parker, M.W., de Silva, M., Lagiakos, H.R., Bentley, J., Pilling, P., Hattarki, M., Dolezal, O., Falk, H., Smyth, G.K., Street, I.P., Monahan, B.J., Peat, T.S., Voss, A.K. & Thomas, T. (2018) Selective inhibition of MYST lysine acetyltransferases leads to cellular senescence in a KAT6-dependent mode. Nature 560, 253-257.
  17. De Luca, A., Parker, L.J., Han, A.W., Rodolfo, C., Gabbarini, V., Hancock, N.C., Palone, F., Mazzetti, A.P., Menin, L., Morton, C.J., Parker, M.W., Lo Bello, M. & Dyson, P. (2019) A structure-based mechanism of cisplatin resistance mediated by Glutathione Transferase P1-1. Proc. Natl. Acad. Sci. USA 116, 13943-13951.
  18. Miles, L.A., Hermans, S., Crespi, G.A.N., Gooi, J.H., Doughty, L., Nero, T.L., Markulić, J., Ebneth, A., Wroblowski, B., Oehlrich, D., Trabanco, A.A., Rives, M-L., Royaux, I., Hancock, N.C., & Parker, M.W. (2019) Small molecule binding to Alzheimer’s risk factor CD33 promotes Abeta phagocytosis. iScience 19, 110-118.