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Dr Paul Curmi
School of Physics
University of New South Wales
Sydney, NSW 2052
Email: p.curmi@unsw.edu.au
Tel: +61-2-9385 4552
Fax: +61-2-9385 6060
Homepage: http://www.phys.unsw.edu.au/STAFF/ACADEMIC/curmi.html

Our principle interest is in the structure, function and evolution of the serpin family of protease inhibitors. We are particularly interested in plasminogen activator inhibitor type 2, where we have solved several crystal structures and are currently probing complexes with interaction partner proteins. The serpin structural transition is part of a larger study that we are undertaking on the characterization of protein motion and transitions. We are also interested in the evolution and spread of the serpin family throughout the evolutionary tree.
Harrop, S., Jankova, L., Coles, M., Whittaker, J., Jardine, D., Gould, A., Meister, A., King, G., Mabbutt, B. and Curmi, P. (1999) The crystal structure of plasminogen activator inhibitor 2: Implications for serpin function. Structure 7, 43-54.

Jankova L, Harrop SJ, Saunders DN, Andrews JL, Bertram KC, Gould AR, Baker MS, Curmi P.M.G. (2001) Crystal structure of the complex of plasminogen activator 2 with a peptide mimicking the reactive center loop. J. Biol. Chem. 276, 43374-82

Saunders DN, Jankova L, Harrop SJ, Curmi, P.M.G., Gould AR, Ranson M, Baker MS. (2001) Interaction between the P14 residue and strand 2 of beta-sheet B is critical for reactive center loop insertion in plasminogen activator inhibitor 2. J. Biol. Chem 276, 43383-9.

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