KEAP1 TEP: Protein Structures and Selectivity Panel for Drug Discovery

University of Oxford researchers present a Target Enabling Package for the KEAP1 protein, a key regulator of cellular stress response. The package includes the first crystal structure of a KEAP1-CUL3 complex and a structure of the apo-Kelch domain suitable for small molecule soaking. It also provides a selectivity assay panel of 17 human Kelch domain-containing proteins, showing high selectivity for KEAP1 inhibitors.

Use Cases

• Virtual screening for KEAP1 inhibitors based on the provided crystal structures.
• Assessing inhibitor selectivity using the panel of 17 human Kelch domain proteins.
• Studying the KEAP1-CUL3 complex structure to understand E3 ligase assembly.
• Designing small molecules for soaking experiments with the apo-Kelch domain structure.
• Researching the redox-sensitive regulation of the KEAP1-NRF2 system for therapeutic development.

Strengths

• Includes the first solved crystal structure of a KEAP1-CUL3 complex.
• Provides a selectivity assay panel covering 17 human Kelch domain proteins.
• Demonstrates high selectivity of known KEAP1 inhibitors against the protein panel.

Limitations

• Row count and dataset size are unknown, which may limit suitability assessment.
• Column-level documentation is absent; field semantics must be inferred after download.
• Last update date is unknown; freshness unverified.

Provenance

Source

R.J. Adamson, University of Oxford, via paperswithcode.

Collection Method

Likely contains structural biology data from crystallography and biochemical assay results.