within the full-length protein the MD-CTD interface appears less flexible and the NTDs are each rotated 90° relative to those in the nucleotide-closed structure of yeast Hsp90. However ...

We determined the structure and function of Heat Shock Protein 90 (Hsp90), a molecular chaperone which is critical for the growth and survival of cancer cells. We worked with partners to discover the ...

HSP90 transits between open and closed states to promote maturation of polypeptide clients into functional proteins with the help of ATP and a variety of co-chaperones. Targeting Hsp90 and its ...

The authors found that the expression of the chaperone protein Hsp90, which helps other proteins acquire their functional shape, was gradually turned down as snowflake yeast evolved larger ...