Structural determination of the A. niger RING finger domain
Abstract
This project addresses the growing global cancer burden by focusing on targeted therapy approaches that disrupt cancer-specific pathways. It investigates the pro-cancer protein RBBP6, specifically the RING domain, which is key to ubiquitination. Unlike the canonical human C3HC4 RING motif, the Aspergillus niger RING domain contains an unusual cysteine-to-aspartic acid substitution, and the aim is to determine its structure to support anti-cancer drug discovery.
Fields of Study & Subjects
Ubiquitin and proteasome pathways
Enzyme Structure and Function
Protein Structure and Dynamics
Publication details
- Journal / source
- European Synchrotron Radiation Facility
- Publication date
- 6 February 2026
- Language
- EN
- Document type
- Dataset