Article
Generation of a Ni(II) binding site by introduction of a histidine cluster in the structure of human glutathione transferase A1-1.
Protein engineering - 1 Nov 1995
Yilmaz S, Widersten M, Emahazion T, Mannervik B
Abstract excerpt
Two mutant forms of human glutathione transferase (GST) A1-1 with affinity for metal ions were constructed by introduction of His residues by site-directed mutagenesis. A mutant, 2-His, contained the mutations Lys84Gln, Asp85His and Glu88His, and another, 5-His, contained the mutations Tyr79His, Asn80His, Lys84His, Asp85His and Glu88His. The mutant proteins were obtained in good yields (40-150 mg per 3 l culture)...
Topics
- Base Sequence
- Binding Sites
- Chromatography, Affinity
- Dinitrochlorobenzene
- Glutathione Transferase
- Histidine
- Humans
- Isoenzymes
- Metalloproteins
- Models, Molecular
- Molecular Sequence Data