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Cryo-EM Structures of Glucocorticoid Receptor-Hsp90-p23 [the GR Maturation Complex], Hsp90-p23, and MBP-Hsp90-p23

ABSTRACT:

SUBMITTER: David Agard

PROVIDER: EMPIAR-11028 | biostudies-other |

REPOSITORIES: biostudies-other

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Structure of Hsp90-p23-GR reveals the Hsp90 client-remodelling mechanism.

Noddings Chari M CM Wang Ray Yu-Ruei RY Johnson Jill L JL Agard David A DA

Nature 20211222 7893

Hsp90 is a conserved and essential molecular chaperone responsible for the folding and activation of hundreds of 'client' proteins1-3. The glucocorticoid receptor (GR) is a model client that constantly depends on Hsp90 for activity4-9. GR ligand binding was previously shown to nr inhibited by Hsp70 and restored by Hsp90, aided by the co-chaperone p2310. However, a molecular understanding of the chaperone-mediated remodelling that occurs between the inactive Hsp70 ...[more]

PMID: 34937936

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