Tertiary interactions stabilise the C-terminal region of human glutathione transferase A1-1: a crystallographic and calorimetric study.

doi:10.1016/j.jmb.2005.04.025

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Article

Tertiary interactions stabilise the C-terminal region of human glutathione transferase A1-1: a crystallographic and calorimetric study.

Journal of molecular biology - 17 Jun 2005

Kuhnert Diane C, Sayed Yasien, Mosebi Salerwe, Sayed Muhammed, Sewell Trevor, Dirr Heini W

Abstract excerpt

The C-terminal region in class Alpha glutathione transferase A1-1 (GSTA1-1), which forms an amphipathic alpha-helix (helix 9), is known to contribute to the catalytic and non-substrate ligand-binding functions of the enzyme. The region in the apo protein is proposed to be disordered which, upon l...

Topics

Binding Sites
Calorimetry
Circular Dichroism
Crystallography, X-Ray
Glutathione
Glutathione Transferase
Humans
Isoenzymes
Isoleucine
Models, Molecular
Mutation
Protein Structure, Tertiary
Protons
Solvents
Temperature
Thermodynamics
Titrimetry
Water

Source

Open in PubMed

Identifiers

PMID: 15893769
DOI: 10.1016/j.jmb.2005.04.025

Genes

GSTA1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-15893769-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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