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Disorder-to-order transition of the active site of human class Pi glutathione transferase, GST P1-1
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Biochemistry.
2001 (English)In: BIOCHEMISTRY, ISSN 0006-2960, Vol. 40, no 39, 11660-11669 p.Article in journal (Refereed) Published
Abstract [en]

Glutathione transferases comprise a large family of cellular detoxification enzymes that function by catalyzing the conjugation of glutathione (GSH) to electron-deficient centers on carcinogens and other toxins. NMR methods have been used to characterize

Place, publisher, year, edition, pages
AMER CHEMICAL SOC , 2001. Vol. 40, no 39, 11660-11669 p.
Keyword [en]
MOLECULAR-DYNAMICS SIMULATIONS; INDUCED-FIT MECHANISM; S-TRANSFERASE; CRYSTAL-STRUCTURE; CATALYTIC MECHANISM; HUMAN PLACENTA; 3-DIMENSIONAL STRUCTURE; ALKYLATING-AGENTS; BREAST-CANCER; NMR-SPECTRA
Identifiers
URN: urn:nbn:se:uu:diva-38016OAI: oai:DiVA.org:uu-38016DiVA: diva2:65915
Note
Addresses: Rule GS, Carnegie Mellon Univ, Dept Biol Sci, 4400 5th Ave, Pittsburgh, PA 15213 USA. Carnegie Mellon Univ, Dept Biol Sci, Pittsburgh, PA 15213 USA. Univ Uppsala, 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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