Human Hsp90-alpha ATPase domain bound to Radicicol
[HS90A_HUMAN] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. 
Publication Abstract from PubMed
CEfrag is a new fragment screening technology based on affinity capillary electrophoresis (ACE). Here we report on the development of a mobility shift competition assay using full-length human heat shock protein 90alpha (Hsp90alpha), radicicol as the competitor probe ligand, and successful screening of the Selcia fragment library. The CEfrag assay was able to detect weaker affinity (IC(50) >500 microM) fragments than were detected by a fluorescence polarization competition assay using FITC-labeled geldanamycin. The binding site of selected fragments was determined by co-crystallization with recombinant Hsp90alpha N-terminal domain and X-ray analysis. The results of this study confirm that CEfrag is a sensitive microscale technique enabling detection of fragments binding to the biological target in near-physiological solution.
Fragment Screening Using Capillary Electrophoresis (CEfrag) for Hit Identification of Heat Shock Protein 90 ATPase Inhibitors.,Austin C, Pettit SN, Magnolo SK, Sanvoisin J, Chen W, Wood SP, Freeman LD, Pengelly RJ, Hughes DE J Biomol Screen. 2012 May 9. PMID:22573733
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.