Human Kalirin/RAC1 GEF Domain Complex: Structural and Activity Data

Experimental data from a programme exploring new ways of targeting GTPases. The dataset contains information on the cloned, expressed, purified, and crystallised first DH GEF domain of Kalirin in complex with RAC1, including results from fragment screening, X-ray crystallography to identify binders, and a developed nucleotide exchange assay establishing GEF activity.

Use Cases

• [Fragment-based drug discovery] based on identified binders within the orthosteric binding site.
• [Structural analysis of protein-protein interactions] based on the crystallised GEF domain complex with RAC1.
• [Validating guanine nucleotide exchange factor (GEF) activity] based on the developed nucleotide exchange assay.
• [Target identification for GTPase modulation] based on the exploration of a new targeting method.

Strengths

• Data is derived from direct experimental methods including protein cloning, purification, and X-ray crystallography.
• Includes functional validation through a developed nucleotide exchange assay establishing GEF activity.
• Available under an Open Access (green) license, facilitating reuse.

Limitations

• Key metadata such as row count, column names, dataset size, and last update date are consistently missing across all source entries.
• The dataset's structure and specific data points (e.g., binding affinities, structural coordinates) are not described.
• Platform tags include irrelevant categories like 'Business' and 'Computer science', suggesting poor curation or keyword stuffing.

Provenance

Source

Janine L. Gray, University of Oxford

Collection Method

Experimental: cloning, expression, purification, crystallization, fragment screening, X-ray crystallography, and biochemical assay development.