Structural and Thermodynamic Insights into Dimerization Interfaces of Drosophila Glutathione Transferases.
Biomolecules
; 14(7)2024 Jun 26.
Article
em En
| MEDLINE
| ID: mdl-39062472
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 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.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Termodinâmica
/
Multimerização Proteica
/
Glutationa Transferase
Limite:
Animals
Idioma:
En
Ano de publicação:
2024
Tipo de documento:
Article