Aurora-A Kinase Fragment Screening with Shape-Diverse Compounds

A fragment set of 80 highly three-dimensional molecular scaffolds was screened against Aurora-A kinase using high-throughput protein crystallography. The work was conducted by Richard Bayliss at the University of Leeds. Four fragment hits were identified that target the allosteric regulator binding site.

Use Cases

• Training models for fragment binding prediction based on three-dimensional scaffold properties.
• Analyzing structure-activity relationships for allosteric kinase inhibitors based on crystallographic hit data.
• Benchmarking virtual screening methods against a shape-diverse fragment collection.

Strengths

• The fragment set consists of 80 compounds, with shape diversity enriched by twenty synthesized fragments.
• Four confirmed crystallographic hits provide a basis for validating computational predictions.

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count for the underlying experimental data is unknown, which may limit suitability assessment.
• Last update date is unknown; freshness unverified.

Provenance

Source

University of Leeds

Collection Method

High-throughput protein crystallography screening of a synthesized fragment library.