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Article

Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis.

The EMBO journal - 7 Feb 2007

Ottmann Christian, Yasmin Lubna, Weyand Michael, Veesenmeyer Jeffrey L, Diaz Maureen H, Palmer Ruth H, Francis Matthew S, Hauser Alan R, Wittinghofer Alfred, Hallberg Bengt

Abstract excerpt

14-3-3 proteins are phosphoserine/phosphothreonine-recognizing adapter proteins that regulate the activity of a vast array of targets. There are also examples of 14-3-3 proteins binding their targets via unphosphorylated motifs. Here we present a structural and biological investigation of the phosphorylation-independent interaction between 14-3-3 and exoenzyme S (ExoS), an ADP-ribosyltransferase toxin of...

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Identifiers

PMID: 17235285
DOI: 10.1038/sj.emboj.7601530
PMCID: PMC1794388

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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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