Naslov
Porcine class pi glutathione S-transferase : anionic-ligand binding and conformational analysis

Autori
Bico, P. ; Erhardt, Julija ; Kaplan, W. ; Dirr, H.

Izvornik
Biochimica et Biophysica Acta : Protein Structure & Molecular Enzymology (0167-4838) 1247 (1995), 2; 225-230

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
glutathione s-transferase. ligand binding. protein conformation

Sažetak
The equilibrium binding of the non-substrate ligands 8-anilino-1-naphthalene sulfonate and bromosulfophthalein to porcine class rr glutathione S-transferase (pGSTP1-1) was studied using a variety of techniques (size-exclusion HPLC, steady-state fluorescence, second-derivative spectroscopy, and chemical modification of cysteines). Both ligands share the same binding site which has a highly hydrophobic surface. Occupation of the site inhibits catalytic function with glutathione and 1-chloro-2, 4-dinitrobenzene in a non-competitive manner. Data obtained from different structural probes either located at strategic regions of pGSTP1-1(Trp-28, Trp-38 and Cys-45) or distributed throughout the protein molecule (tyrosine residues) suggest that binding induces a microstructural change that impacts on the functional conformation of the active site. [References: 35]

Izvorni jezik
Engleski

Znanstvena područja
Biologija

POVEZANOST RADA