BAIT

GSTP1

DFN7, FAEES3, GST3, GSTP, HEL-S-22, PI
glutathione S-transferase pi 1
GO Process (30)
GO Function (7)
GO Component (9)

Gene Ontology Biological Process

Homo sapiens
PREY

GSTP1

DFN7, FAEES3, GST3, GSTP, HEL-S-22, PI
glutathione S-transferase pi 1
GO Process (30)
GO Function (7)
GO Component (9)

Gene Ontology Biological Process

Homo sapiens

Reconstituted Complex

An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.

Publication

Direct evidence for the formation of a complex between 1-cysteine peroxiredoxin and glutathione S-transferase pi with activity changes in both enzymes.

Ralat LA, Manevich Y, Fisher AB, Colman RF

Glutathione S-transferase pi (GST pi) has been shown to reactivate oxidized 1-cysteine peroxiredoxin (1-Cys Prx, Prx VI, Prdx6, and AOP2). We now demonstrate that a heterodimer complex is formed between 1-Cys Prx with a C-terminal His6 tag and GST pi upon incubation of the two proteins at pH 8.0 in buffer containing 20% 1,6-hexanediol to dissociate the homodimers, followed by ... [more]

Biochemistry Jan. 17, 2006; 45(2);360-72 [Pubmed: 16401067]

Throughput

  • Low Throughput

Additional Notes

  • Figure 1
  • homodimer

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
GSTP1 GSTP1
Co-crystal Structure
Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Low-BioGRID
-

Curated By

  • BioGRID