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Article

Calorimetric and structural studies of the nitric oxide carrier S-nitrosoglutathione bound to human glutathione transferase P1-1.

Protein science : a publication of the Protein Society - 1 May 2006

Téllez-Sanz Ramiro, Cesareo Eleonora, Nuccetelli Marzia, Aguilera Ana M, Barón Carmen, Parker Lorien J, Adams Julian J, Morton Craig J, Lo Bello Mario, Parker Michael W, García-Fuentes Luis

Abstract excerpt

The nitric oxide molecule (NO) is involved in many important physiological processes and seems to be stabilized by reduced thiol species, such as S-nitrosoglutathione (GSNO). GSNO binds strongly to glutathione transferases, a major superfamily of detoxifying enzymes. We have determined the crystal structure of GSNO bound to dimeric human glutathione transferase P1-1 (hGSTP1-1) at 1.4 A resolution. The GSNO ligand...

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Identifiers

PMID: 16597834
DOI: 10.1110/ps.052055206
PMCID: PMC2242504

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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