Structural and Thermodynamic Insights into Dimerization Interfaces of Drosophila Glutathione Transferases.

Autor: Schwartz M; Flavour Perception: Molecular Mechanisms (Flavours), INRAE, CNRS, Université de Bourgogne, 21000 Dijon, France., Petiot N; Laboratoire Interdisciplinaire Carnot de Bourgogne, UMR 6303 CNRS, Université de Bourgogne Franche-Comté, 21078 Dijon, France., Chaloyard J; Flavour Perception: Molecular Mechanisms (Flavours), INRAE, CNRS, Université de Bourgogne, 21000 Dijon, France., Senty-Segault V; Flavour Perception: Molecular Mechanisms (Flavours), INRAE, CNRS, Université de Bourgogne, 21000 Dijon, France., Lirussi F; UMR 1231, Lipides Nutrition Cancer, INSERM, 21000 Dijon, France.; UFR des Sciences de Santé, Université de Bourgogne Franche-Comté, 25000 Besançon, France.; Plateforme PACE, Laboratoire de Pharmacologie-Toxicologie, Centre Hospitalo-Universitaire Besançon, 25000 Besançon, France., Senet P; Laboratoire Interdisciplinaire Carnot de Bourgogne, UMR 6303 CNRS, Université de Bourgogne Franche-Comté, 21078 Dijon, France., Nicolai A; Laboratoire Interdisciplinaire Carnot de Bourgogne, UMR 6303 CNRS, Université de Bourgogne Franche-Comté, 21078 Dijon, France., Heydel JM; Flavour Perception: Molecular Mechanisms (Flavours), INRAE, CNRS, Université de Bourgogne, 21000 Dijon, France., Canon F; Independent Researcher, 21000 Dijon, France., Sonkaria S; Soft Foundry Institute, Seoul National University, Kwanak-gu, Seoul 39-131, Republic of Korea., Khare V; Soft Foundry Institute, Seoul National University, Kwanak-gu, Seoul 39-131, Republic of Korea., Didierjean C; CRM2 Laboratory, CNRS, Université de Lorraine, 54000 Nancy, France., Neiers F; Flavour Perception: Molecular Mechanisms (Flavours), INRAE, CNRS, Université de Bourgogne, 21000 Dijon, France.
Jazyk: angličtina
Zdroj: Biomolecules [Biomolecules] 2024 Jun 26; Vol. 14 (7). Date of Electronic Publication: 2024 Jun 26.
DOI: 10.3390/biom14070758
Abstrakt: This study presents a comprehensive analysis of the dimerization interfaces of fly GSTs through sequence alignment. Our investigation revealed GSTE1 as a particularly intriguing target, providing valuable insights into the variations within Delta and Epsilon GST interfaces. The X-ray structure of GSTE1 was determined, unveiling remarkable thermal stability and a distinctive dimerization interface. Utilizing circular dichroism, we assessed the thermal stability of GSTE1 and other Drosophila GSTs with resolved X-ray structures. The subsequent examination of GST dimer stability correlated with the dimerization interface supported by findings from X-ray structural analysis and thermal stability measurements. Our discussion extends to the broader context of GST dimer interfaces, offering a generalized perspective on their stability. This research enhances our understanding of the structural and thermodynamic aspects of GST dimerization, contributing valuable insights to the field.
Databáze: MEDLINE
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