11gs

Glutathione s-transferase complexed with ethacrynic acid-glutathione conjugate (form ii)

spinqualitylabelsall models 11gs, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 11gs is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EAA, GSH, MES Gene: GSTP1 (HUMAN) Activity: Glutathione transferase, with EC number 2.5.1.18 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [GSTP1_HUMAN] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The diuretic drug ethacrynic acid, an inhibitor of pi class glutathione S-transferase, has been tested in clinical trials as an adjuvant in chemotherapy. We recently solved the crystal structure of this enzyme in complex with ethacrynic acid and its glutathione conjugate. Here we present a new structure of the ethacrynic-glutathione conjugate complex. In this structure the ethacrynic moiety of the complex is shown to bind in a completely different orientation to that previously observed. Thus there are at least two binding modes possible, an observation of great importance to the design of second generation inhibitors of the enzyme. The glutathione conjugate of ethacrynic acid can bind to human pi class glutathione transferase P1-1 in two different modes.,Oakley AJ, Lo Bello M, Mazzetti AP, Federici G, Parker MW FEBS Lett. 1997 Dec 8;419(1):32-6. PMID:9426214 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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