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Capturing the Conformational Ensemble of the Mixed Folded Polyglutamine Protein Ataxin-3.
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- Author(s): Sicorello A;Sicorello A;Sicorello A; Różycki B; Różycki B; Konarev PV; Konarev PV; Svergun DI; Svergun DI; Pastore A; Pastore A; Pastore A
- Source:
Structure (London, England : 1993) [Structure] 2021 Jan 07; Vol. 29 (1), pp. 70-81.e5. Date of Electronic Publication: 2020 Oct 15.- Publication Type:
Journal Article; Research Support, Non-U.S. Gov't- Language:
English - Source:
- Additional Information
- Source: Publisher: Cell Press Country of Publication: United States NLM ID: 101087697 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1878-4186 (Electronic) Linking ISSN: 09692126 NLM ISO Abbreviation: Structure Subsets: MEDLINE
- Publication Information: Publication: 2000- : Cambridge, Mass. : Cell Press
Original Publication: London : Current Biology, c1993- - Subject Terms:
- Abstract: Ataxin-3 is a deubiquitinase involved in protein quality control and other essential cellular functions. It preferentially interacts with polyubiquitin chains of four or more units attached to proteins delivered to the ubiquitin-proteasome system. Ataxin-3 is composed of an N-terminal Josephin domain and a flexible C terminus that contains two or three ubiquitin-interacting motifs (UIMs) and a polyglutamine tract, which, when expanded beyond a threshold, leads to protein aggregation and misfolding and causes spinocerebellar ataxia type 3. The high-resolution structure of the Josephin domain is available, but the structural and dynamical heterogeneity of ataxin-3 has so far hindered the structural description of the full-length protein. Here, we characterize non-expanded and expanded variants of ataxin-3 in terms of conformational ensembles adopted by the proteins in solution by jointly using experimental data from nuclear magnetic resonance and small-angle X-ray scattering with coarse-grained simulations. Our results pave the way to a molecular understanding of polyubiquitin recognition.
Competing Interests: Declaration of Interests The authors declare absence of any conflict of interest.
(Copyright © 2020 Elsevier Ltd. All rights reserved.) - Grant Information: FC001029 United Kingdom Wellcome Trust; FC001029 United Kingdom CRUK_ Cancer Research UK; MC_U117533887 United Kingdom MRC_ Medical Research Council; MC_PC_13054 United Kingdom MRC_ Medical Research Council; FC001029 United Kingdom MRC_ Medical Research Council
- Contributed Indexing: Keywords: Monte Carlo simulations; NMR; PRE; SAXS; ensemble refinement; hybrid methods; intrinsically unfolded proteins; neurodegeneration; polyglutamine
- Accession Number: 0 (Peptides)
26700-71-0 (polyglutamine)
EC 3.4.19.12 (Ataxin-3) - Publication Date: Date Created: 20201016 Date Completed: 20211123 Latest Revision: 20220129
- Publication Date: 20240105
- Accession Number: 10.1016/j.str.2020.09.010
- Accession Number: 33065068
- Source:
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