Highlights d p53 requires Hsp70 and Hsp90 for regulating its DNA binding activity d Hsp70 inactivates p53 at physiological temperatures by unfolding it d Hsp90 folds p53 to native conformation in an ATP-dependent process d p53 conformation constantly switches between Hsp70-and Hsp90-bound states

The small heat shock protein (sHsp) αA-crystallin is a molecular chaperone important for the optical properties of the vertebrate eye lens. It forms heterogeneous oligomeric ensembles. We determined the structures of human αA-crystallin oligomers combining cryo-electron microscopy, cross-linking/mass spectrometry, nuclear magnetic resonance spectroscopy and molecular modeling. The different oligomers can be interconverted by the addition or subtraction of Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:

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