The dimeric state of glutathione transferases; role of a key residue at the subunit interface in human GSTP1-1

Authors
Stenberg, G Abdallah, AM Mannervik, B
Citation
G. Stenberg et al., The dimeric state of glutathione transferases; role of a key residue at the subunit interface in human GSTP1-1, CHEM-BIO IN, 133(1-3), 2001, pp. 24-27
Citations number
14
Categorie Soggetti
Pharmacology & Toxicology
Journal title
CHEMICO-BIOLOGICAL INTERACTIONS
ISSN journal
00092797 → ACNP
Volume
133
Issue
1-3
Year of publication
2001
Pages
24 - 27
Database
ISI
SICI code
0009-2797(20010228)133:1-3<24:TDSOGT>2.0.ZU;2-D
Abstract
The dimer interface has been modified in human GSTP1-1 by site-directed mut agenesis. Five single-point mutants were generated by the exchange of Tyr50 , the key residue in the lock-and-key motif, for Ala, Arg, Phe, Leu and Thr . Both structural stabilities as well as catalytic function are affected by the mutations. The levels of soluble protein are significantly reduced for the Tyr50Ala and Tyr50Arg mutants but essentially unchanged for the other variants. (C) 2001 Elsevier Science Ireland Ltd. All rights reserved.