Michael Parker laboratory
Professor Michael Parker
+61 3 83442211
Proteins are one of the body's most essential building blocks and are the molecular engines that control all functions of the body. X-ray crystallography offers the means to view the three-dimensional structure of proteins at the atomic level. Since the majority of drugs interact with proteins, crystal structures have proved to be invaluable for the discovery and development of new drugs.
The work of our laboratory is internationally recognised with the determination of more than one hundred crystal structures including those of membrane-associating proteins, detoxifying enzymes and protein kinases. This work has provided insights into a number of diseases such as cancer, bacterial and viral infections, and neurological diseases such as Alzheimer's disease. In recent years we have been emphasising the translational aspects of our work with an increasing focus on structure-based drug discovery. This focus has been underpinned by the development of virtual screening and fragment screening platforms in-house, by funding from the Australian Cancer Research Foundation, and partnerships with a number of Biotechnology companies including CSL Limited and Janssen.
Keywords: Protein structure, X-ray crystallography, Structure-based drug design, Cancer, Alzheimer’s Disease, Parkinson’s Disease, Bacterial toxins
Saira Batool, Honours Student
Camille Braganca, Honours Student
Dr Michelle Christie, Post-doctoral Fellow
Karen Steffi Cheung Tung Shing, Post-doctoral Fellow
Gabriella Crespi, Research Assistant
Larissa Doughty, Facility Manager
Marialena Georgopoulou, PhD Student
Dr Jonathan Gooi, Laboratory Manager
Dr Michael Gorman, Post-doctoral Fellow
Nancy Hancock, Research Assistant
Dr Stefan Hermans, Post-doctoral Fellow
Kenta Ishii, MSc Student
Bronte Johnstone, PhD Student
Dr Belinda Michell, Laboratory Manager
Dr Craig Morton, Post-doctoral Fellow
Dr Tracy Nero, Post-doctoral Fellow
Dr Claire Weekley, Post-doctoral Fellow
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- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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., Gomez, G.A., Alexandrov, K., Wilson, I.A., Doxastakis, M., Mark, A.E. & Waters, M.J. (2014) Mechanism of activation of protein kinase JAK2 by the growth hormone receptor. Science 344, 710
- 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.
- Baell, J.B., Leaver, D., Cleary, B., Nguyen, N., 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.
- 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 Aβ phagocytosis. iScience 19, 110-118.
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