High-Affinity Ligand Binding Data for Human UBR2 Ubiquitin Ligase

Experimental data on high-affinity small-molecule ligands developed for the human ubiquitin E3 ligase UBR2. The dataset likely contains binding affinity measurements (Kd ∼ 20–40 nM) and selectivity data against the homologue UBR1, derived from a peptidomimetic approach incorporating unnatural amino acids. The data was authored by Shih-Ting Huang and shared on figshare in May 2026.

Use Cases

• Training models to predict protein-ligand binding affinity based on peptidomimetic structures.
• Analyzing selectivity profiles between homologous proteins UBR2 and UBR1.
• Supporting structure-based drug design for UBR box-containing E3 ligases based on high-resolution cocrystal structures (~1.2 Å).
• Investigating molecular mechanisms of high-affinity binding for tripeptide ligands.

Strengths

• Includes high-resolution cocrystal structures at approximately 1.2 Å resolution.
• Reports ligand binding affinities with Kd values in the 20–40 nM range.
• Demonstrates 10-fold selectivity for UBR2 over its closest homologue, UBR1.

Limitations

• Row count is unknown, which may limit suitability assessment.
• Column-level documentation is absent; field semantics must be inferred after download.
• Dataset is very small at 2.6 KB, indicating limited scope.

Provenance

Source

figshare

Collection Method

Experimental data from a peptidomimetic approach and structural analysis.

Time Range

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Freshness

Last updated 2026-05-08 20:29:29; freshness should be verified.

Geography

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