Ternary degradation complexes and independent controls
Research context
study · conditional · As of 2026-10-10
peer reviewed · 2017-03-13
- Study design
- Crystal structure with ITC, surface mutagenesis, proximity assays and selected cellular degradation measurements.
- Reported result
- Supports cooperative ternary recognition and selective Brd4 depletion for studied compounds.
- Limitations
- Abstract and detailed figure captions inspected; no universal ligand/ligase or clinical-function generalization.
Gadd and colleagues resolved a Brd4 bromodomain–MZ1–VHL complex and combined binding, mutagenesis, proximity and cell-protein measurements.
Key knowledge
Gadd and colleagues resolved a Brd4 bromodomain–MZ1–VHL complex and combined binding, mutagenesis, proximity and cell-protein measurements. Cooperative ternary recruitment can help explain selectivity in that system; binary affinity alone does not establish degradation efficiency or phenotype specificity.
Conditions and scope
- The studied bromodomain/ligase/compounds and cellular assays bound the conclusion; a proximity-signal decline can be an assay hook effect rather than loss of ternary complexes.
Sources · 1
References
Sources retain their recorded scope. A source link alone does not establish verification of every statement.
Evidence and review
Structural basis of PROTAC cooperative recognition for selective protein degradation: Original abstract and figure captions: Brd4 BD2/MZ1/VHL structure, ITC/mutagenesis/proximity and cellular degradation (original abstract and detailed original figure captions, not complete online methods)
2026-10-10 · Bounded author source inspection of ternary degradation complexes and independent controls, including the stated conditions; independent branch review is recorded separately.
Entry details
Permanent link to this entry ↗- Record identity
- res-chem-protac-ternary
- Revision
- research.1
- Structured reference record
- Postgraduate & research reference