L. Roeglin, Philipp Thiel, O. Kohlbacher
May 1, 2012
Citations
0
Influential Citations
16
Citations
Journal
Proceedings of the National Academy of Sciences
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 14-3-3ζ 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.