α-Synuclein mutations cluster around a putative protein loop()

With the recent identification of two new pathogenic mutations in α-synuclein, we map the five known pathogenic mutations onto the best available models of the protein structure. We show that four of the five mutations map to a potential fold in the protein with the exception being the A30P mutation...

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Autores principales: Kara, Eleanna, Lewis, Patrick A., Ling, Helen, Proukakis, Christos, Houlden, Henry, Hardy, John
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Scientific Publishers Ireland 2013
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3694303/
https://www.ncbi.nlm.nih.gov/pubmed/23669636
http://dx.doi.org/10.1016/j.neulet.2013.04.058
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author Kara, Eleanna
Lewis, Patrick A.
Ling, Helen
Proukakis, Christos
Houlden, Henry
Hardy, John
author_facet Kara, Eleanna
Lewis, Patrick A.
Ling, Helen
Proukakis, Christos
Houlden, Henry
Hardy, John
author_sort Kara, Eleanna
collection PubMed
description With the recent identification of two new pathogenic mutations in α-synuclein, we map the five known pathogenic mutations onto the best available models of the protein structure. We show that four of the five mutations map to a potential fold in the protein with the exception being the A30P mutation in which the substitution would be expected to have a profound effect on protein structure. We discuss this localisation in terms of the proposed mechanisms for mutation pathogenicity.
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spelling pubmed-36943032013-06-27 α-Synuclein mutations cluster around a putative protein loop() Kara, Eleanna Lewis, Patrick A. Ling, Helen Proukakis, Christos Houlden, Henry Hardy, John Neurosci Lett Article With the recent identification of two new pathogenic mutations in α-synuclein, we map the five known pathogenic mutations onto the best available models of the protein structure. We show that four of the five mutations map to a potential fold in the protein with the exception being the A30P mutation in which the substitution would be expected to have a profound effect on protein structure. We discuss this localisation in terms of the proposed mechanisms for mutation pathogenicity. Elsevier Scientific Publishers Ireland 2013-06-24 /pmc/articles/PMC3694303/ /pubmed/23669636 http://dx.doi.org/10.1016/j.neulet.2013.04.058 Text en © 2013 The Authors https://creativecommons.org/licenses/by/3.0/ Open Access under CC BY 3.0 (https://creativecommons.org/licenses/by/3.0/) license
spellingShingle Article
Kara, Eleanna
Lewis, Patrick A.
Ling, Helen
Proukakis, Christos
Houlden, Henry
Hardy, John
α-Synuclein mutations cluster around a putative protein loop()
title α-Synuclein mutations cluster around a putative protein loop()
title_full α-Synuclein mutations cluster around a putative protein loop()
title_fullStr α-Synuclein mutations cluster around a putative protein loop()
title_full_unstemmed α-Synuclein mutations cluster around a putative protein loop()
title_short α-Synuclein mutations cluster around a putative protein loop()
title_sort α-synuclein mutations cluster around a putative protein loop()
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3694303/
https://www.ncbi.nlm.nih.gov/pubmed/23669636
http://dx.doi.org/10.1016/j.neulet.2013.04.058
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