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Article

Mutations of Gly to Ala in human glutathione transferase P1-1 affect helix 2 (G-site) and induce positive cooperativity in the binding of glutathione.

Journal of molecular biology - 18 Dec 1998

Lo Bello M, Nuccetelli M, Chiessi E, Lahm A, Mazzetti A P, Battistoni A, Caccuri A M, Oakley A J, Parker M W, Tramontano A, Federici G, Ricci G

Abstract excerpt

Previous kinetic studies on human glutathione transferase P1-1 have indicated that the motions of an irregular alpha-helix (helix 2) lining the glutathione (GSH) binding site are viscosity dependent and may modulate the affinity of GSH binding. The effect of single amino acid residue substitutions (Gly to Ala) in this region is investigated here by site-directed mutagenesis. Three mutants (Gly41Ala, Gly50Ala and...

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PMID: 9878382
DOI: 10.1006/jmbi.1998.2270

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Mutations of Gly to Ala in human glutathione transferase P1-1 affect helix 2 (G-site) and induce positive cooperativity in the binding of glutathione.PMID 9878382Read ↗

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