UCL logo

UCL Discovery

UCL home » Library Services » Electronic resources » UCL Discovery

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.

Full text not available from this repository.

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
URI: http://discovery.ucl.ac.uk/id/eprint/145893
Downloads since deposit
0Downloads
Download activity - last month
Download activity - last 12 months
Downloads by country - last 12 months

Archive Staff Only

View Item View Item