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Protein Engineering, Vol. 15, No. 10, 827-834, October 2002
© 2002 Oxford University Press

Design of a monomeric human glutathione transferase GSTP1, a structurally stable but catalytically inactive protein

Abdel-Monem Abdalla1,2, Christopher M. Bruns1,3, John A. Tainer1,3, Bengt Mannervik1 and Gun Stenberg1,4

1 Department of Biochemistry, Uppsala University, Biomedical Center,Box 576, SE-75123 Uppsala, Sweden and 3 Department of Molecular Biology MB4, Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, CA 92037, USA

By the introduction of 10 site-specific mutations in the dimer interface of human glutathione transferase P1-1 (GSTP1-1), a stable monomeric protein variant, GSTP1, was obtained. The monomer had lost the catalytic activity but retained the affinity for a number of electrophilic compounds normally serving as substrates for GSTP1-1. Fluorescence and circular dichroism spectra of the monomer and wild-type proteins were similar, indicating that there are no large structural differences between the subunits of the respective proteins. The GSTs have potential as targets for in vitro evolution and redesign with the aim of developing proteins with novel properties. To this end, a monomeric GST variant may have distinct advantages.


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