5x79
From Proteopedia
Human GST Pi conjugated with novel inhibitor, GS-ESF
Structural highlights
FunctionGSTP1_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.[1] Publication Abstract from PubMedWe 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Homo sapiens | Large Structures | Abe H | Fukui K | Kimura Y | Shishido Y | Tomoike F
