5x79

Human GST Pi conjugated with novel inhibitor, GS-ESF

spinqualitylabelsall models 5x79, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5x79 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: GF5, MES 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. Publication Abstract from PubMed We herein report the first covalent G-site-binding inhibitor for GST, GS-ESF (1), which irreversibly inhibited the GSTP1-1 function. LC-MS/MS and X-ray structure analyses of the covalently linked GST-inhibitor complex suggested that 1 reacted with Tyr108 of GSTP1-1. The mechanism of covalent bond formation was discussed based on MD simulation results. A covalent G-site inhibitor for glutathione S-transferase Pi (GSTP1-1).,Shishido Y, Tomoike F, Kimura Y, Kuwata K, Yano T, Fukui K, Fujikawa H, Sekido Y, Murakami-Tonami Y, Kameda T, Shuto S, Abe H Chem Commun (Camb). 2017 Aug 29. doi: 10.1039/c7cc05829b. PMID:28848941 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glutathione S-transferase 3D structures

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