[HTML][HTML] The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation

JP Grenert, WP Sullivan, P Fadden… - Journal of Biological …, 1997 - ASBMB
Many functions of the chaperone, heat shock protein 90 (hsp90), are inhibited by the drug
geldanamycin that specifically binds hsp90. We have studied an amino-terminal domain of
hsp90 whose crystal structure has recently been solved and determined to contain a
geldanamycin-binding site. We demonstrate that, in solution, drug binding is exclusive to this
domain. This domain also binds ATP linked to Sepharose through the γ-phosphate. Binding
is specific for ATP and ADP and is inhibited by geldanamycin. Mutation of four glycine …