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Article

Binding features of chloroplast fructose-1,6-bisphosphatase-thioredoxin interaction.

Biochimica et biophysica acta - 5 May 2001

Wangensteen O S, Chueca A, Hirasawa M, Sahrawy M, Knaff D B, López Gorgé J

Abstract excerpt

It has been proposed that a hydrophobic groove surrounded by positively charged amino acids on thioredoxin (Trx) serves as the recognition and docking site for the interaction of Trx with target proteins. This model for Trx-protein interactions fits well with the Trx-mediated fructose-1,6-bisphosphatase (FBPase) activation, where a protruding negatively charged loop of FBPase would bind to this Trx groove, in a...

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PMID: 11343801
DOI: 10.1016/s0167-4838(01)00178-9

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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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