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The client protein p53 adopts a molten globule-like state in the presence of hsp90

Academic Article
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Overview

authors

  • Park, S. J.
  • Borin, B. N.
  • Martinez-Yamout, M. A.
  • Dyson, Jane

publication date

  • May 2011

journal

  • Nature Structural & Molecular Biology  Journal

abstract

  • It is not currently known in what state (folded, unfolded or alternatively folded) client proteins interact with the chaperone Hsp90. We show that one client, the p53 DNA-binding domain, undergoes a structural change in the presence of Hsp90 to adopt a molten globule-like state. Addition of one- and two-domain constructs of Hsp90, as well as the full-length three-domain protein, to isotopically labeled p53 led to reduction in NMR signal intensity throughout p53, particularly in its central β-sheet. This reduction seems to be associated with a change of structure of p53 without formation of a distinct complex with Hsp90. Fluorescence and hydrogen-exchange measurements support a loosening of the structure of p53 in the presence of Hsp90 and its domains. We propose that Hsp90 interacts with p53 by multiple transient interactions, forming a dynamic heterogeneous manifold of conformational states that resembles a molten globule.

subject areas

  • Amino Acid Sequence
  • Binding Sites
  • HSP90 Heat-Shock Proteins
  • Humans
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Folding
  • Protein Structure, Tertiary
  • Spectrometry, Fluorescence
  • Tumor Suppressor Protein p53
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Identity

PubMed Central ID

  • PMC3087862

International Standard Serial Number (ISSN)

  • 1545-9985

Digital Object Identifier (DOI)

  • 10.1038/nsmb.2045

PubMed ID

  • 21460846
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Additional Document Info

start page

  • 537

end page

  • 541

volume

  • 18

issue

  • 5

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