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Dr James C Whisstock
Department of Biochemistry and Molecular Biology
Monash University
PO Box 13d, Melbourne, Vic 3800
Email: James.Whisstock@med.monash.edu.au
Tel: +61-3 9905 3747
Fax: +61-3 9905 4699
Homepage:

Research
The primary focus of my groups research is the structure and function of the serpin superfamily of protease inhibitors and their interactions with target proteases. In particular, the work aims to characterise the molecular mechanism of the nuclear cysteine protease inhibitor MENT and its interaction with chromatin. In addition, we have recently discovered several members of the serpin superfamily in thermphilic bacteria and archae. We have determined the X-ray crystal structure of a number of these molecules with the goal of understanding how serpins have adapted to a heated enviroment.
Collaborations
Rob Pike
Steve Bottomley
Phil Bird
Eleanor Mackie
Sergei Grigoryev
Chris Mitchell
Michael Berndt
Jamie Rossjohn
Gary Silverman
Publications
Irving JA, Cabrita LD, Rossjohn J, Pike RN, Bottomley SP, Whisstock JC.The 1.5 A crystal structure of a prokaryote serpin: controlling conformational change in a heated environment. Structure (Camb). 2003

Irving JA, Steenbakkers PJ, Lesk AM, Op den Camp HJ, Pike RN, Whisstock JC.Serpins in prokaryotes.Mol Biol Evol. 2002

Irving JA, Shushanov SS, Pike RN, Popova EY, Bromme D, Coetzer TH, Bottomley SP, Boulynko IA, Grigoryev SA, Whisstock JC.Inhibitory activity of a heterochromatin-associated serpin (MENT) against papain-like cysteine proteinases affects chromatin structure and blocks cell proliferation.J Biol Chem. 2002 Apr 12; 277(15): 13192-201.

J.A. Irving, R.N. Pike, A.M. Lesk, and J.C. Whisstock. "Phylogeny of the Serpin Superfamily: Implications of patterns of amino acids conservation for structure and function". Genome Res. 12: 1845-1864 (2000).

Silverman GA, Bird PI, Carrell RW, Church FC, Coughlin PB, Gettins PG, Irving JA, Lomas DA, Luke CJ, Moyer RW, Pemberton PA, Remold-O'Donnell E, Salvesen GS, Travis J,
Whisstock JC.The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature.J Biol Chem. 2001





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