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Article

Crystal structure of the PP2A phosphatase activator: implications for its PP2A-specific PPIase activity.

Molecular cell - 4 Aug 2006

Leulliot Nicolas, Vicentini Giorgia, Jordens Jan, Quevillon-Cheruel Sophie, Schiltz Marc, Barford David, van Tilbeurgh Herman, Goris Jozef

Abstract excerpt

PTPA, an essential and specific activator of protein phosphatase 2A (PP2A), functions as a peptidyl prolyl isomerase (PPIase). We present here the crystal structures of human PTPA and of the two yeast orthologs (Ypa1 and Ypa2), revealing an all alpha-helical protein fold that is radically different from other PPIases. The protein is organized into two domains separated by a groove lined by highly conserved...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 16885030
DOI: 10.1016/j.molcel.2006.07.008

Genes

PTPA

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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