Role of mutation Y6F on the binding properties of Schistosoma japonicum glutathione S-transferase

Yassin, Zeyad; Ortiz‐Salmerón, Emilia; Clemente-Jimenez, M.Jose; Barón, Carmen; Garcı́a-Fuentes, Luis

doi:10.1016/s0141-8130(03)00039-4

Cited by 5 publications

(1 citation statement)

References 28 publications

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“…However, most GSH simulations demonstrate GSH prefers to stay in the G-site. In human and rat, Y6 contributes to the stabilization of the thiol group [ 40 ], whereas Y115 involves the addition of GSH to xenobiotic and product release [ 41 ]. These residues are also conserved in RmGST (Y7 and Y116).…”

Section: Resultsmentioning

confidence: 99%

Observing How Glutathione and S-Hexyl Glutathione Bind to Glutathione S-Transferase from Rhipicephalus (Boophilus) microplus

Rangubpit

Suwan

Sangthong

et al. 2022

IJMS

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Rhipicephalus (Boophilus) microplus is one of the most widespread ticks causing a massive loss to livestock production. The long-term use of acaracides rapidly develops acaracide resistance. In R. microplus, enhancing the metabolic activity of glutathione S-transferase (RmGST) is one of the mechanisms underlying acaracide resistance. RmGST catalyzes the conjugation of glutathione (GSH) to insecticides causing an easy-to-excrete conjugate. The active RmGST dimer contains two active sites (hydrophobic co-substrate binding site (H-site) and GSH binding site (G-site)) in each monomer. To preserve the insecticide efficacy, s-hexyl glutathione (GTX), a GST inhibitor, has been used as a synergist. To date, no molecular information on the RmGST-GSH/GTX complex is available. The insight is important for developing a novel RmGST inhibitor. Therefore, in this work, molecular dynamics simulations (MD) were performed to explore the binding of GTX and GSH to RmGST. GSH binds tighter and sits rigidly inside the G-site, while flexible GTX occupies both active sites. In GSH, the backbone mainly interacts with W8, R43, W46, K50, N59, L60, Q72, and S73, while its thiol group directs to Y7. In contrast, the aliphatic hexyl of GTX protrudes into the H-site and allows a flexible peptide core to form various interactions. Such high GTX flexibility and the protrusion of its hexyl moiety to the H-site suggest the dual role of GTX in preventing the conjugation reaction and the binding of acaracide. This insight can provide a better understanding of an important insecticide-resistance mechanism, which may in turn facilitate the development of novel approaches to tick control.

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Section: Resultsmentioning

confidence: 99%

Observing How Glutathione and S-Hexyl Glutathione Bind to Glutathione S-Transferase from Rhipicephalus (Boophilus) microplus

Rangubpit

Suwan

Sangthong

et al. 2022

IJMS

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A survey of the year 2003 literature on applications of isothermal titration calorimetry

Cliff

Gutiérrez

Ladbury

2004

J of Molecular Recognition

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Over the last decade isothermal titration calorimetry (ITC) has developed from a specialist method which was largely restricted in its use to dedicated experts, to a major, commercially available tool in the arsenal directed at understanding molecular interactions. The number of those proficient in this field has multiplied dramatically, as has the range of experiments to which this method has been applied. This has led to an overwhelming amount of new data and novel applications to be assessed. With the increasing number of publications in this field comes a need to highlight works of interest and impact. In this overview of the literature we have attempted to draw attention to papers and issues for which both the experienced calorimetrist and the interested dilettante hopefully will share our enthusiasm.

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A monomer form of the glutathione S-transferase Y7F mutant from Schistosoma japonicum at acidic pH

Andújar‐Sánchez

Clemente-Jiménez

Rodríguez‐Vico

et al. 2004

Biochemical and Biophysical Research Communications

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Role of mutation Y6F on the binding properties of Schistosoma japonicum glutathione S-transferase

Cited by 5 publications

References 28 publications

Observing How Glutathione and S-Hexyl Glutathione Bind to Glutathione S-Transferase from Rhipicephalus (Boophilus) microplus

Observing How Glutathione and S-Hexyl Glutathione Bind to Glutathione S-Transferase from Rhipicephalus (Boophilus) microplus

A survey of the year 2003 literature on applications of isothermal titration calorimetry

A monomer form of the glutathione S-transferase Y7F mutant from Schistosoma japonicum at acidic pH

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