Peter Colman

Peter Colman

Peter Colman in 2014, portrait via the Royal Society
Born Peter Malcolm Colman
April 3, 1944[1]
Adelaide[2]
Fields
Institutions
Alma mater
Thesis The physical structure of two parabanic acid complexes and an investigation of short intermolecular carbon-oxygen contacts (1969)
Known for
Influences
Notable awards
Website
www.wehi.edu.au/faculty_members/professor_peter_colman

Peter Malcolm Colman (born 1944)[1] FRS is Head of the Structural Biology Division at the The Walter and Eliza Hall Institute of Medical Research in Melbourne, Australia.[8][9]

Education

Colman was educated at the University of Adelaide where he was awarded a Bachelor of Science degree in Physics in 1965 and a PhD in 1969 for research on the chemical structure of parabanic acid complexes .[10]

Research

Colman's research interests are in structural biology,[4][11][12][13][14][15][16][17][18][19] especially of human B-cell lymphoma 2 (BCL-2).[20][21][22][23]

Awards and honours

Peter Colman, showing his flu protein (neuraminidase) model to Frank Macfarlane Burnet.

Colman was elected a Fellow of the Royal Society (FRS) in 2014. His nomination reads:

“ Colman determined the three-dimensional structure of the influenza virus neuraminidase and, in one of the earliest cases of structure-based drug design, discovered zanamivir, the first-in-class Neuraminidase Inhibitor for influenza. His subsequent structural studies on resistance to this drug class suggested how to design drugs against moving targets. His discoveries underpin drug stockpiling for pandemic preparedness. He has made seminal contributions to structural studies of antibodies and antibody-antigen complexes. Recent work on apoptosis solves the long-standing problem of how pro-apoptotic Bax changes conformation to dimerise and then oligomerise and permeabilise the mitochondrial membrane, an essential step in the intrinsic cell-death pathway.[6] ”

Colman was also elected a Fellow of the Australian Academy of Science (FAA) in 1989 and a Fellow of the Australian Academy of Technological Sciences and Engineering (FTSE) in 1997.[1]

References

  1. ↑ 1.0 1.1 1.2 COLMAN, Dr Peter Malcolm. Who's Who 2014 (online Oxford University Press ed.). A & C Black, an imprint of Bloomsbury Publishing plc. (subscription required)
  2. ↑ 2.0 2.1 2.2 2.3 Peter Malcolm Colman, CSIROpedia, Commonwealth Scientific and Industrial Research Organisation
  3. ↑ Colman, P. M. (1994). "Influenza virus neuraminidase: Structure, antibodies, and inhibitors". Protein Science 3 (10): 1687–96. doi:10.1002/pro.5560031007. PMC 2142611. PMID 7849585.
  4. ↑ 4.0 4.1 Huber, R.; Deisenhofer, J.; Colman, P. M.; Matsushima, M.; Palm, W. (1976). "Crystallographic structure studies of an IgG molecule and an Fc fragment". Nature 264 (5585): 415–20. doi:10.1038/264415a0. PMID 1004567.
  5. ↑ Colman, P. M.; Freeman, H. C.; Guss, J. M.; Murata, M.; Norris, V. A.; Ramshaw, J. A. M.; Venkatappa, M. P. (1978). "X-ray crystal structure analysis of plastocyanin at 2.7 Å resolution". Nature 272 (5651): 319. doi:10.1038/272319a0.
  6. ↑ 6.0 6.1 "Professor Peter Colman FRS". London: The Royal Society.
  7. ↑ Professor Peter Colman, Australian Institute of Policy and Science, AIPS
  8. ↑ List of publications from Microsoft Academic Search
  9. ↑ Peter Colman's publications indexed by the Scopus bibliographic database, a service provided by Elsevier.
  10. ↑ Colman, Peter Malcolm (1969). The physical structure of two parabanic acid complexes and an investigation of short intermolecular carbon-oxygen contacts (PhD thesis). University of Adelaide.
  11. ↑ von Itzstein, M.; Wu, W. Y.; Kok, G. B.; Pegg, M. S.; Dyason, J. C.; Jin, B.; Phan, T. V.; Smythe, M. L.; White, H. F.; Oliver, S. W.; Colman, P. M.; Varghese, J. N.; Ryan, D. M.; Woods, J. M.; Bethell, R. C.; Hotham, V. J.; Cameron, J. M.; Penn, C. R. (1993). "Rational design of potent sialidase-based inhibitors of influenza virus replication". Nature 363 (6428): 418–23. doi:10.1038/363418a0. PMID 8502295.
  12. ↑ Chothia, C.; Lesk, A. M.; Tramontano, A.; Levitt, M.; Smith-Gill, S. J.; Air, G.; Sheriff, S.; Padlan, E. A.; Davies, D.; Tulip, W. R.; Colman, P. M.; Spinelli, S.; Alzari, P. M.; Poljak, R. J. (1989). "Conformations of immunoglobulin hypervariable regions". Nature 342 (6252): 877–883. Bibcode:1989Natur.342..877C. doi:10.1038/342877a0. PMID 2687698.
  13. ↑ Lawrence, M. C.; Colman, P. M. (1993). "Shape Complementarity at Protein/Protein Interfaces". Journal of Molecular Biology 234 (4): 946. doi:10.1006/jmbi.1993.1648. PMID 8263940.
  14. ↑ Varghese, J. N.; Laver, W. G.; Colman, P. M. (1983). "Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution". Nature 303 (5912): 35–40. doi:10.1038/303035a0. PMID 6843658.
  15. ↑ Colman, P. M. (1994). "Effects of amino acid sequence changes on antibody-antigen interactions". Research in Immunology 145 (1): 33–6. doi:10.1016/S0923-2494(94)80039-1. PMID 7516563.
  16. ↑ Colman, P. M.; Lawrence, M. C. (2003). "The structural biology of type I viral membrane fusion". Nature Reviews Molecular Cell Biology 4 (4): 309–19. doi:10.1038/nrm1076. PMID 12671653.
  17. ↑ Colman, P. M.; Laver, W. G.; Varghese, J. N.; Baker, A. T.; Tulloch, P. A.; Air, G. M.; Webster, R. G. (1987). "Three-dimensional structure of a complex of antibody with influenza virus neuraminidase". Nature 326 (6111): 358. doi:10.1038/326358a0. PMID 2436051.
  18. ↑ Type 1 Diabetes Research Update - with Professor Peter Colman on YouTube
  19. ↑ Colman, P. M.; Varghese, J. N.; Laver, W. G. (1983). "Structure of the catalytic and antigenic sites in influenza virus neuraminidase". Nature 303 (5912): 41–4. doi:10.1038/303041a0. PMID 6188957.
  20. ↑ Lessene, G.; Czabotar, P. E.; Colman, P. M. (2008). "BCL-2 family antagonists for cancer therapy". Nature Reviews Drug Discovery 7 (12): 989. doi:10.1038/nrd2658. PMID 19043450.
  21. ↑ Brady, R. M.; Vom, A.; Roy, M. J.; Toovey, N.; Smith, B. J.; Moss, R. M.; Hatzis, E.; Huang, D. C. S.; Parisot, J. P.; Yang, H.; Street, I. P.; Colman, P. M.; Czabotar, P. E.; Baell, J. B.; Lessene, G. (2014). "De-Novo Designed Library of Benzoylureas as Inhibitors of BCL-XL: Synthesis, Structural and Biochemical Characterization". Journal of Medicinal Chemistry 57 (4): 1323. doi:10.1021/jm401948b. PMID 24456288.
  22. ↑ Koehler, M. F. T.; Bergeron, P.; Choo, E. F.; Lau, K.; Ndubaku, C.; Dudley, D.; Gibbons, P.; Sleebs, B. E.; Rye, C. S.; Nikolakopoulos, G.; Bui, C.; Kulasegaram, S.; Kersten, W. J. A.; Smith, B. J.; Czabotar, P. E.; Colman, P. M.; Huang, D. C. S.; Baell, J. B.; Watson, K. G.; Hasvold, L.; Tao, Z. F.; Wang, L.; Souers, A. J.; Elmore, S. W.; Flygare, J. A.; Fairbrother, W. J.; Lessene, G. (2014). "Structure-Guided Rescaffolding of Selective Antagonists of BCL-XL". ACS Medicinal Chemistry Letters 5 (6): 662. doi:10.1021/ml500030p. PMID 24944740.
  23. ↑ Chen, L.; Willis, S. N.; Wei, A.; Smith, B. J.; Fletcher, J. I.; Hinds, M. G.; Colman, P. M.; Day, C. L.; Adams, J. M.; Huang, D. C. S. (2005). "Differential Targeting of Prosurvival Bcl-2 Proteins by Their BH3-Only Ligands Allows Complementary Apoptotic Function". Molecular Cell 17 (3): 393–403. doi:10.1016/j.molcel.2004.12.030. PMID 15694340.