Crystal Structures of Human HSP90alpha Complexed with Dihydroxyphenylpyrazole Inhibitors

Andreas Kreusch from the Genomics Institute of the Novartis Research Foundation provides crystal structures for two dihydroxyphenylpyrazole compounds complexed with the N-terminal ATP binding domain of human Hsp90alpha. The description details specific molecular interactions, such as hydrogen bonds between the compounds and amino acid residues Asp93, Gly97, and Thr184. One compound, G3130, demonstrated cellular activities consistent with Hsp90 inhibition.

Use Cases

• Analyzing protein-ligand binding interactions based on described hydrogen bonds with Asp93, Gly97, and Thr184.
• Training machine learning models for virtual screening based on structural features of reversible Hsp90 inhibitors.
• Studying molecular docking poses for dihydroxyphenylpyrazole compounds in the adenine binding pocket.
• Validating computational chemistry predictions against experimental crystallographic data for Hsp90alpha complexes.

Strengths

• Structures reveal specific atomic-level interactions, including a direct hydrogen bond between the C2 hydroxyl group and the side chain of Asp93.
• The description includes a specific compound identifier (G3130) with associated cellular activity data for validation.

Limitations

• Row count and dataset scale are unknown, which may limit suitability assessment.
• Column-level documentation is absent; field semantics must be inferred after download.
• Last update date is unknown; freshness unverified.

Provenance

Source

Genomics Institute of the Novartis Research Foundation

Collection Method

X-ray crystallography