Covalent attachment of pyridoxalphosphate derivatives to 14-3-3 proteins

L. Roglin, P. Thiel, O. Kohlbacher, C. Ottmann

Research output: Contribution to journalArticlepeer-review

16 Citations (Scopus)
2 Downloads (Pure)

Abstract

Small-molecule inhibitors of 14-3-3 protein–protein interactions could serve as valuable chemical biology tools and starting points for drug development. The article by Zhao et al. (1) described FOBISIN101 (1) (Fig. 1A), a pyridoxal-phosphate (PLP) derivative that inhibits 14-3-3 protein–protein interactions. The authors provided a crystal structure of 14-3-3¿ with PLP covalently bound to K120 [Protein Data Bank (PDB) ID code 3RDH] lacking the p-amino-benzoate moiety. As a mechanism, they propose X-ray–induced cleavage of the N=N bond. They suggest this mechanism could serve as a radiation-triggered anticancer prodrug concept.
Original languageEnglish
Pages (from-to)E1051-E1053
Number of pages3
JournalProceedings of the National Academy of Sciences of the United States of America (PNAS)
Volume109
Issue number18
DOIs
Publication statusPublished - 2012

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