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The dimeric state of glutathione transferases; role of a key residue at the subunit interface in human GSTP1-1
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Biochemistry.
2001 (English)In: CHEMICO-BIOLOGICAL INTERACTIONS, ISSN 0009-2797, Vol. 133, no 1-3, 24-27 p.Article in journal (Refereed) Published
Abstract [en]

The dimer interface has been modified in human GSTP1-1 by site-directed mutagenesis. 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

Place, publisher, year, edition, pages
ELSEVIER SCI IRELAND LTD , 2001. Vol. 133, no 1-3, 24-27 p.
Keyword [en]
glutathione transferase; interface; mutagenesis; folding-assembly; S-TRANSFERASE; POSITIVE COOPERATIVITY; MECHANISM; P1-1; EVOLUTION; STABILITY; COMPLEX; A1-1; SITE
URN: urn:nbn:se:uu:diva-38039OAI: oai:DiVA.org:uu-38039DiVA: diva2:65938
Addresses: Stenberg G, Uppsala Univ, Biomed Ctr, Dept Biochem, Box 576, SE-75123 Uppsala, Sweden. Uppsala Univ, Biomed Ctr, Dept Biochem, SE-75123 Uppsala, Sweden.Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-14

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