ParkinsonFranceV1, Ncbi, Curation, bibRecord, 000A19

Structural characterization of α-synuclein in an aggregation prone state

Identifieur interne : 000A19 ( Ncbi/Curation ); précédent : 000A18; suivant : 000A20

Structural characterization of α-synuclein in an aggregation prone state

Auteurs : Min-Kyu Cho [Allemagne] ; Gabrielle Nodet [France] ; Hai-Young Kim [Allemagne] ; Malene R. Jensen [France] ; Pau Bernado [Espagne] ; Claudio O. Fernandez [Argentine] ; Stefan Becker [Allemagne] ; Martin Blackledge [France] ; Markus Zweckstetter [Allemagne]

Source :

Protein Science : A Publication of the Protein Society [ 0961-8368 ] ; 2009.

RBID : PMC:2777359

Abstract

The relation of α-synuclein (αS) aggregation to Parkinson's disease has long been recognized, but the pathogenic species and its molecular properties have yet to be identified. To obtain insight into the properties of αS in an aggregation-prone state, we studied the structural properties of αS at acidic pH using NMR spectroscopy and computation. NMR demonstrated that αS remains natively unfolded at lower pH, but secondary structure propensities were changed in proximity to acidic residues. The ensemble of conformations of αS at acidic pH is characterized by a rigidification and compaction of the Asp and Glu-rich C-terminal region, an increased probability for proximity between the NAC-region and the C-terminal region and a lower probability for interactions between the N- and C-terminal regions.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2777359

DOI: 10.1002/pro.194
PubMed: 19554627
PubMed Central: 2777359

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PMC:2777359

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<front><div type="abstract" xml:lang="en"><p>The relation of α-synuclein (αS) aggregation to Parkinson's disease has long been recognized, but the pathogenic species and its molecular properties have yet to be identified. To obtain insight into the properties of αS in an aggregation-prone state, we studied the structural properties of αS at acidic pH using NMR spectroscopy and computation. NMR demonstrated that αS remains natively unfolded at lower pH, but secondary structure propensities were changed in proximity to acidic residues. The ensemble of conformations of αS at acidic pH is characterized by a rigidification and compaction of the Asp and Glu-rich C-terminal region, an increased probability for proximity between the NAC-region and the C-terminal region and a lower probability for interactions between the N- and C-terminal regions.</p>
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	La maladie de Parkinson en France (serveur d'exploration)
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La maladie de Parkinson en France (serveur d'exploration)

Structural characterization of α-synuclein in an aggregation prone state

Structural characterization of α-synuclein in an aggregation prone state

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Abstract

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