Molecular dynamics investigation of single nucleotide polymorphism-driven variations in GSTP1 phosphorylation and substrate interaction.

doi:10.1080/07391102.2026.2619869

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Article

Molecular dynamics investigation of single nucleotide polymorphism-driven variations in GSTP1 phosphorylation and substrate interaction.

Journal of biomolecular structure & dynamics - 1 Jun 2026

Shahwar Durr-E-, Usama, Khan Zahid, Ahmad Naveed, Ali Aktar, Imran Muhammad

Abstract excerpt

This study evaluated the impact of the rs1695 (Ile105Val) substitution on GSTP1 structural stability, phosphorylation accessibility, and interaction with ethacrynic acid (EA), as a substrate. Molecular dynamics (MD) simulations were conducted for wild-type (WT) and Val105 mutant GSTP1 variants using the CHARMM36m force field in GROMACS. EA was docked to phosphorylated models, followed by 100 ns MD simulations...

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Identifiers

PMID: 41569518
DOI: 10.1080/07391102.2026.2619869

Genes

GSTP1

Variants

rs1695

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

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