Structural highlights
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.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sun KH, Chang KH, Clawson S, Ghosh S, Mirzaei H, Regnier F, Shah K. Glutathione-S-transferase P1 is a critical regulator of Cdk5 kinase activity. J Neurochem. 2011 Sep;118(5):902-14. doi: 10.1111/j.1471-4159.2011.07343.x. Epub , 2011 Jul 8. PMID:21668448 doi:10.1111/j.1471-4159.2011.07343.x
- ↑ 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. A covalent G-site inhibitor for glutathione S-transferase Pi (GSTP1-1). Chem Commun (Camb). 2017 Aug 29. doi: 10.1039/c7cc05829b. PMID:28848941 doi:http://dx.doi.org/10.1039/c7cc05829b
