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Publication Abstract from PubMed

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.

Structural and Thermodynamic Insights into Dimerization Interfaces of Drosophila Glutathione Transferases.,Schwartz M, Petiot N, Chaloyard J, Senty-Segault V, Lirussi F, Senet P, Nicolai A, Heydel JM, Canon F, Sonkaria S, Khare V, Didierjean C, Neiers F Biomolecules. 2024 Jun 26;14(7):758. doi: 10.3390/biom14070758. PMID:39062472^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.