Jump to main content
Jump to site search


A covalent G-site inhibitor for glutathione S-transferase Pi (GSTP1-1)

Author affiliations

Abstract

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.

Graphical abstract: A covalent G-site inhibitor for glutathione S-transferase Pi (GSTP1-1)

Back to tab navigation

Supplementary files

Publication details

The article was received on 26 Jul 2017, accepted on 19 Aug 2017 and first published on 21 Aug 2017


Article type: Communication
DOI: 10.1039/C7CC05829B
Citation: Chem. Commun., 2017, Advance Article
  •   Request permissions

    A covalent G-site inhibitor for glutathione S-transferase Pi (GSTP1-1)

    Y. Shishido, F. Tomoike, Y. Kimura, K. Kuwata, T. Yano, K. Fukui, H. Fujikawa, Y. Sekido, Y. Murakami-Tonami, T. Kameda, S. Shuto and H. Abe, Chem. Commun., 2017, Advance Article , DOI: 10.1039/C7CC05829B

Search articles by author

Spotlight

Advertisements