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Article

A conserved "hydrophobic staple motif" plays a crucial role in the refolding of human glutathione transferase P1-1.

The Journal of biological chemistry - 7 Apr 2000

Stenberg G, Dragani B, Cocco R, Mannervik B, Aceto A

Abstract excerpt

The specific (i, i+5) hydrophobic staple interaction involving a helix residue and a second residue located in the turn preceding the helix is a recurrent motif at the N terminus of alpha-helices. This motif is strictly conserved in the core of all soluble glutathione transferases (GSTs) as well as in other protein structures. Human GSTP1-1 variants mutated in amino acid Ile(149) and Tyr(154) of the hydrophobic...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 10744731
DOI: 10.1074/jbc.275.14.10421

Genes

GSTP1

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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A conserved "hydrophobic staple motif" plays a crucial role in the refolding of human glutathione transferase P1-1.PMID 10744731Read ↗

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