Supplementary Figure 3: Nucleotide binding does not promote allosteric changes in the Hsp90–M-TTR complex.
From Mechanistic basis for the recognition of a misfolded protein by the molecular chaperone Hsp90
- Journal name:
- Nature Structural & Molecular Biology
- Year published:
- DOI:
- doi:10.1038/nsmb.3380
Additional data
Author footnotes
These authors contributed equally to this work.
- Javier Oroz &
- Jin Hae Kim
Affiliations
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German Center for Neurodegenerative Diseases (DZNE), Göttingen, Germany.
- Javier Oroz,
- Jin Hae Kim &
- Markus Zweckstetter
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Department for NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
- Bliss J Chang &
- Markus Zweckstetter
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Department of Neurology, University Medical Center Göttingen, University of Göttingen, Göttingen, Germany.
- Markus Zweckstetter
Contributions
J.H.K. performed NMR spectroscopy and biochemical experiments on TTR variants, as well as structure calculations. J.O. performed NMR spectroscopy, SAXS and ITC experiments on Hsp90. B.J.C. and J.O. produced Hsp90 mutants for the assignment of isoleucine methyl groups. J.H.K., J.O. and M.Z. designed experiments. J.H.K., J.O. and M.Z. wrote the paper.
Competing financial interests
The authors declare no competing financial interests.
Author details
Javier Oroz
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Jin Hae Kim
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Bliss J Chang
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Markus Zweckstetter
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Supplementary Figure 1: The structure of the misfolded monomeric conformation of TTR is well defined.Hover over figure to zoom
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Supplementary Figure 2: Reproducibility in calorimetric titrations of Hsp90 with M-TTR.Hover over figure to zoom
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Supplementary Figure 3: Nucleotide binding does not promote allosteric changes in the Hsp90–M-TTR complex.Hover over figure to zoom
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Supplementary Figure 4: Hsp90 uses several binding interfaces to bind M-TTR.Hover over figure to zoom