HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Lewis, P. A. Articles by Jackson, G. S. Search for Related Content PubMed PubMed Citation Articles by Lewis, P. A. Articles by Jackson, G. S. Agricola Articles by Lewis, P. A. Articles by Jackson, G. S.

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

MRC Prion Unit, Department of Neurodegenerative Disease, Institute of Neurology, University College London, Queen Square, London WC1N 3BG, UK

Correspondence
Graham S. Jackson
g.s.jackson{at}prion.ucl.ac.uk

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 (PrP^C). Here, it is shown that the polymorphism does not change the efficiency of conversion to the -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.

This article has been cited by other articles:

				C. M. Ott, A. Akhavan, and V. R. Lingappa Specific Features of the Prion Protein Transmembrane Domain Regulate Nascent Chain Orientation J. Biol. Chem., April 13, 2007; 282(15): 11163 - 11171. [Abstract] [Full Text] [PDF]