Binding Affinity Data for Crk/CrkL SH2 Domain Antagonist Peptides

A structure–function relationship study by Taeju Park, last updated in 2026, designed peptides with higher binding affinities to Crk and CrkL SH2 domains. The dataset includes results from saturation transfer difference NMR, fluorescence polarization, and FP competition assays. It demonstrates that substituting amino acids at specific positions improves the binding affinity of YXXP motif-containing peptides.

Use Cases

• Training models to predict peptide binding affinity based on amino acid substitutions.
• Benchmarking computational molecular modeling results against experimental binding assays.
• Identifying lead compounds for inhibiting Crk/CrkL-mediated protein–protein interactions in cancer.

Strengths

• Data is derived from multiple experimental methods: STD-NMR, fluorescence polarization, and FP competition assays.
• The study includes a clear structure–function relationship framework with two rounds of amino acid substitution.
• Dataset is associated with a specific, peer-reviewed research goal: developing inhibitors for Crk and CrkL.

Limitations

• Row count is unknown, which may limit suitability assessment.
• Column-level documentation is absent; field semantics must be inferred after download.
• The dataset is very small at 25.3 KB, indicating a limited scope of experimental results.

Provenance

Source

figshare

Collection Method

Experimental data from molecular modeling, STD-NMR, and fluorescence polarization assays.

Freshness

Last updated 2026-04-20 23:44:59; freshness should be verified.