Targeting a Pleckstrin Homology Domain: Covalent Binder Structures and Binding Data

Rebekah M. West's dataset on figshare contains research data for a novel approach to inhibiting Bruton's Tyrosine Kinase (BTK) by targeting its PH domain. The dataset, last updated in May 2026, includes 27 crystal structures and structure-binding relationship data for a fragment that covalently modifies a lysine in the PIP3 binding site. The 4.2 MB ZIP file is shared under a CC-BY-NC-4.0 license.

Use Cases

• Analyzing structure-activity relationships based on the 27 crystal structures mentioned in the description.
• Modeling covalent inhibitor binding to PH domains based on the described lysine-targeting fragment.
• Comparing PIP3 analog binding inhibition across different PH domains as suggested by the pKa evaluation.
• Developing novel kinase inhibitors that avoid the conserved ATP binding site, as explored in the study.

Strengths

• Includes 27 crystal structures, providing a detailed structural basis for analysis.
• Focuses on a novel inhibition strategy targeting the PH domain, a less conserved site than the ATP binding pocket.
• Dataset is relatively small at 4.2 MB, facilitating quick download and inspection.

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment for statistical tasks.
• Description metadata is limited; actual data quality and completeness require manual inspection.

Provenance

Source

figshare, author Rebekah M. West.

Collection Method

Likely contains experimental data from fragment screening, crystallography, and binding assays.

Time Range

null

Freshness

Last updated 2026-05-14 08:30:32; freshness should be verified.

Geography

null