Stebbins et al. reported novel JNK inhibitors that block JNK binding to the scaffolding protein JIP1 (1). The most potent compound, BI-78D3, was postulated to bind noncovalently toJNK at the JIP1 site. The binding data and structure of BI-78D3 suggest, however, that BI-78D3 may instead act throughcovalent modification of JNK at Cys163. (Cys163 is referredto as Cys162 in ref. 1. See www.uniprot.org/uniprot/P45983).
展开▼
