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Codon 129 polymorphism of the human prion protein influences the kinetics of amyloid formation

Lewis, PA; Tattum, MH; Jones, S; Bhelt, D; Batchelor, M; Clarke, AR; Collinge, J; (2006) Codon 129 polymorphism of the human prion protein influences the kinetics of amyloid formation. J GEN VIROL , 87 2443 - 2449. 10.1099/vir.0.81630-0.

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Abstract

The human prion protein (PrP) has a common polymorphism at residue 129, which can be valine or methionine. This polymorphism has a strong influence on susceptibility to prion diseases and on prion-strain properties. Previous work has shown that this amino acid variation has no measurable effect on the native structure of cellular PrP (PrPC). Here, it is shown that the polymorphism does not change the efficiency of conversion to the beta-PrP conformation or affect the binding of copper(II) ions. However, in a partially denatured conformation, the polymorphic variation has a profound influence on the ability of the protein to form amyloid fibrils spontaneously.

Type: Article
Title: Codon 129 polymorphism of the human prion protein influences the kinetics of amyloid formation
DOI: 10.1099/vir.0.81630-0
Keywords: CREUTZFELDT-JAKOB-DISEASE, FATAL FAMILIAL INSOMNIA, VARIANT CJD, DNA POLYMORPHISM, GENE, SCRAPIE, SUSCEPTIBILITY, CONVERSION, PHENOTYPE, GENOTYPE
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences > UCL Institute of Prion Diseases
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences > UCL Institute of Prion Diseases > MRC Prion Unit at UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences > UCL Queen Square Institute of Neurology
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences > UCL Queen Square Institute of Neurology > Department of Neuromuscular Diseases
URI: http://discovery.ucl.ac.uk/id/eprint/145893
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