1BGQ

RADICICOL BOUND TO THE ATP BINDING SITE OF THE N-TERMINAL DOMAIN OF THE YEAST HSP90 CHAPERONE

Summary for 1BGQ

• Entry DOI: 10.2210/pdb1bgq/pdb
• Descriptor: HEAT SHOCK PROTEIN 90, RADICICOL (3 entities in total)
• Functional Keywords: chaperone, atp-binding, heat shock, inhibitor
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm: P02829
• Total number of polymer chains: 1
• Total formula weight: 25891.81

Authors

Roe, S.M.,Prodromou, C.,Pearl, L.H. (deposition date: 1998-05-29, release date: 1999-06-08, Last modification date: 2024-05-22)

Primary citation

Roe, S.M.,Prodromou, C.,O'Brien, R.,Ladbury, J.E.,Piper, P.W.,Pearl, L.H.
Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin.
J.Med.Chem., 42:260-266, 1999

PubMed Abstract: The cellular activity of several regulatory and signal transduction proteins, which depend on the Hsp90 molecular chaperone for folding, is markedly decreased by geldanamycin and by radicicol (monorden). We now show that these unrelated compounds both bind to the N-terminal ATP/ADP-binding domain of Hsp90, with radicicol displaying nanomolar affinity, and both inhibit the inherent ATPase activity of Hsp90 which is essential for its function in vivo. Crystal structure determinations of Hsp90 N-terminal domain complexes with geldanamycin and radicicol identify key aspects of their nucleotide mimicry and suggest a rational basis for the design of novel antichaperone drugs.

PubMed: 9925731
DOI: 10.1021/jm980403y

Experimental method

X-RAY DIFFRACTION (2.5 Å)