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000139178 041__ $$aEnglish
000139178 082__ $$a570
000139178 1001_ $$0P:(DE-2719)2810826$$aOroz, Javier$$b0$$eFirst author$$udzne
000139178 245__ $$aMechanistic basis for the recognition of a misfolded protein by the molecular chaperone Hsp90.
000139178 260__ $$aLondon [u.a.]$$bNature Publishing Group$$c2017
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000139178 520__ $$aThe critical toxic species in over 40 human diseases are misfolded proteins. Their interaction with molecular chaperones such as Hsp90, which preferentially interacts with metastable proteins, is essential for the blocking of disease progression. Here we used nuclear magnetic resonance (NMR) spectroscopy to determine the three-dimensional structure of the misfolded cytotoxic monomer of the amyloidogenic human protein transthyretin, which is characterized by the release of the C-terminal β-strand and perturbations of the A-B loop. The misfolded transthyretin monomer, but not the wild-type protein, binds to human Hsp90. In the bound state, the Hsp90 dimer predominantly populates an open conformation, and transthyretin retains its globular structure. The interaction surface for the transthyretin monomer comprises the N-terminal and middle domains of Hsp90 and overlaps with that of the Alzheimer's-disease-related protein tau. Taken together, the data suggest that Hsp90 uses a mechanism for the recognition of aggregation-prone proteins that is largely distinct from those of other Hsp90 clients.
000139178 536__ $$0G:(DE-HGF)POF3-342$$a342 - Disease Mechanisms and Model Systems (POF3-342)$$cPOF3-342$$fPOF III$$x0
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000139178 650_7 $$2NLM Chemicals$$aHSP90 Heat-Shock Proteins
000139178 650_7 $$2NLM Chemicals$$aIntrinsically Disordered Proteins
000139178 650_7 $$2NLM Chemicals$$aMolecular Chaperones
000139178 650_7 $$2NLM Chemicals$$aPrealbumin
000139178 650_7 $$2NLM Chemicals$$atau Proteins
000139178 650_2 $$2MeSH$$aHSP90 Heat-Shock Proteins: chemistry
000139178 650_2 $$2MeSH$$aHSP90 Heat-Shock Proteins: metabolism
000139178 650_2 $$2MeSH$$aHumans
000139178 650_2 $$2MeSH$$aImaging, Three-Dimensional
000139178 650_2 $$2MeSH$$aIntrinsically Disordered Proteins: chemistry
000139178 650_2 $$2MeSH$$aIntrinsically Disordered Proteins: metabolism
000139178 650_2 $$2MeSH$$aMagnetic Resonance Spectroscopy
000139178 650_2 $$2MeSH$$aModels, Biological
000139178 650_2 $$2MeSH$$aModels, Molecular
000139178 650_2 $$2MeSH$$aMolecular Chaperones: chemistry
000139178 650_2 $$2MeSH$$aMolecular Chaperones: metabolism
000139178 650_2 $$2MeSH$$aPrealbumin: chemistry
000139178 650_2 $$2MeSH$$aPrealbumin: metabolism
000139178 650_2 $$2MeSH$$aProtein Binding
000139178 650_2 $$2MeSH$$aProtein Conformation
000139178 650_2 $$2MeSH$$aProtein Folding
000139178 650_2 $$2MeSH$$aProtein Multimerization
000139178 650_2 $$2MeSH$$atau Proteins: chemistry
000139178 650_2 $$2MeSH$$atau Proteins: metabolism
000139178 7001_ $$0P:(DE-2719)9000457$$aKim, Jin Hae$$b1$$udzne
000139178 7001_ $$0P:(DE-HGF)0$$aChang, Bliss J$$b2
000139178 7001_ $$0P:(DE-2719)2810591$$aZweckstetter, Markus$$b3$$eLast author$$udzne
000139178 77318 $$2Crossref$$3journal-article$$a10.1038/nsmb.3380$$b : Springer Science and Business Media LLC, 2017-02-20$$n4$$p407-413$$tNature Structural & Molecular Biology$$v24$$x1545-9993$$y2017
000139178 773__ $$0PERI:(DE-600)2131437-8$$a10.1038/nsmb.3380$$gVol. 24, no. 4, p. 407 - 413$$n4$$p407-413$$q24:4<407 - 413$$tNature structural & molecular biology$$v24$$x1545-9993$$y2017
000139178 8564_ $$uhttps://www.nature.com/articles/nsmb.3380
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000139178 9141_ $$y2017
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