La maladie de Parkinson en France (serveur d'exploration)

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Molecular Interaction between the Chaperone Hsc70 and the N-terminal Flank of Huntingtin Exon 1 Modulates Aggregation*

Identifieur interne : 001601 ( Ncbi/Curation ); précédent : 001600; suivant : 001602

Molecular Interaction between the Chaperone Hsc70 and the N-terminal Flank of Huntingtin Exon 1 Modulates Aggregation*

Auteurs : Elodie Monsellier [France] ; Virginie Redeker [France] ; Gemma Ruiz-Arlandis [France] ; Luc Bousset [France] ; Ronald Melki [France]

Source :

RBID : PMC:4317008

Abstract

Background: Hsc70 has an alleviating effect on the toxicity of polyglutamine (polyQ)-containing proteins in vivo.

Results: Hsc70 binds specifically the N-terminal flank of huntingtin exon 1.

Conclusion: Hsc70 interaction with huntingtin exon 1 N-terminal flank affects the conformation of the resulting assemblies.

Significance: We identify the surface interfaces between Hsc70 and huntingtin exon 1, which allows the design of future therapeutic tools.


Url:
DOI: 10.1074/jbc.M114.603332
PubMed: 25505179
PubMed Central: 4317008

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PMC:4317008

Le document en format XML

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<bold>Background:</bold>
Hsc70 has an alleviating effect on the toxicity of polyglutamine (polyQ)-containing proteins
<italic>in vivo</italic>
.</p>
<p>
<bold>Results:</bold>
Hsc70 binds specifically the N-terminal flank of huntingtin exon 1.</p>
<p>
<bold>Conclusion:</bold>
Hsc70 interaction with huntingtin exon 1 N-terminal flank affects the conformation of the resulting assemblies.</p>
<p>
<bold>Significance:</bold>
We identify the surface interfaces between Hsc70 and huntingtin exon 1, which allows the design of future therapeutic tools.</p>
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