Journal article

Human theta class glutathione transferase: the crystal structure reveals a sulfate-binding pocket within a buried active site

J Rossjohn, WJ McKinstry, AJ Oakley, D Verger, J Flanagan, G Chelvanayagam, KL Tan, PG Board, MW Parker

Structure | CELL PRESS | Published : 1998

Abstract

BACKGROUND: Glutathione S-transferases (GSTs) comprise a multifunctional group of enzymes that play a critical role in the cellular detoxification process. These enzymes reduce the reactivity of toxic compounds by catalyzing their conjugation with glutathione. As a result of their role in detoxification, GSTs have been implicated in the development of cellular resistance to antibiotics, herbicides and clinical drugs and their study is therefore of much interest. In mammals, the cytosolic GSTs can be divided into five distinct classes termed alpha, mu, pi, sigma and theta. The human theta class GST, hGST T2-2, possesses several distinctive features compared to GSTs of other classes, including..

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