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

ABSTRACT: 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 gene

SUBMITTER: Schwartz M 

PROVIDER: S-EPMC11274453 | biostudies-literature | 2024 Jun

REPOSITORIES: biostudies-literature