{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["5"],"submitter":["De Luca A"],"pubmed_abstract":["We provide the first biochemical evidence of a direct interaction between the glutathione transferase P1-1 (GSTP1-1) and the TRAF domain of TNF receptor-associated factor 2 (TRAF2), and describe how ligand binding modulates such an equilibrium. The dissociation constant of the heterocomplex is K(d)=0.3 μM; however the binding affinity strongly decreases when the active site of GSTP1-1 is occupied by the substrate GSH (K(d)≥2.6 μM) or is inactivated by oxidation (Kd=1.7 μM). This indicates that GSTP1-1's TRAF2-binding region involves the GSH-binding site. The GSTP1-1 inhibitor NBDHEX further decreases the complex's binding affinity, as compared with when GSH is the only ligand; this suggests that the hydrophobic portion of the GSTP1-1 active site also contributes to the interaction. We ther"],"journal":["Cell death & disease"],"pagination":["e1015"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4040697"],"repository":["biostudies-literature"],"pubmed_title":["The fine-tuning of TRAF2-GSTP1-1 interaction: effect of ligand binding and in situ detection of the complex."],"pmcid":["PMC4040697"],"pubmed_authors":["Mei G","Nicolai E","Pastore A","Serra M","Federici L","Palumbo C","Rosato N","De Luca A","Caccuri AM"],"additional_accession":[]},"is_claimable":false,"name":"The fine-tuning of TRAF2-GSTP1-1 interaction: effect of ligand binding and in situ detection of the complex.","description":"We provide the first biochemical evidence of a direct interaction between the glutathione transferase P1-1 (GSTP1-1) and the TRAF domain of TNF receptor-associated factor 2 (TRAF2), and describe how ligand binding modulates such an equilibrium. The dissociation constant of the heterocomplex is K(d)=0.3 μM; however the binding affinity strongly decreases when the active site of GSTP1-1 is occupied by the substrate GSH (K(d)≥2.6 μM) or is inactivated by oxidation (Kd=1.7 μM). This indicates that GSTP1-1's TRAF2-binding region involves the GSH-binding site. The GSTP1-1 inhibitor NBDHEX further decreases the complex's binding affinity, as compared with when GSH is the only ligand; this suggests that the hydrophobic portion of the GSTP1-1 active site also contributes to the interaction. We ther","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Jan","modification":"2025-04-04T22:59:00.096Z","creation":"2019-03-27T01:29:15Z"},"accession":"S-EPMC4040697","cross_references":{"pubmed":["24457959"],"doi":["10.1038/cddis.2013.529"]}}