Crystal structure of the eIF4A-PDCD4 complex

摘要: Tumor suppressor programmed cell death protein 4 (PDCD4) inhibits the translation initiation factor eIF4A, an RNA helicase that catalyzes unwinding of secondary structure at 5′-untranslated region mRNAs and controls translation. Here, we determined crystal human eIF4A PDCD4 complex. The reveals one molecule binds to two molecules through different binding modes. While MA3 domains bind molecule, C-terminal domain alone same also interacts with another molecule. eIF4A–PDCD4 complex suggests domain(s) perpendicular interface preventing closure blocking both which are required events in function helicase. structure, together biochemical analyses, insights into inhibition mechanism by provides a framework for designing chemicals target eIF4A.