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Article

Conformational diversity in prion protein variants influences intermolecular beta-sheet formation.

The EMBO journal - 6 Jan 2010

Lee Seungjoo, Antony Lizamma, Hartmann Rune, Knaus Karen J, Surewicz Krystyna, Surewicz Witold K, Yee Vivien C

Abstract excerpt

A conformational transition of normal cellular prion protein (PrP(C)) to its pathogenic form (PrP(Sc)) is believed to be a central event in the transmission of the devastating neurological diseases known as spongiform encephalopathies. The common methionine/valine polymorphism at residue 129 in the PrP influences disease susceptibility and phenotype. We report here seven crystal structures of human PrP variants:...

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Source

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Identifiers

PMID: 19927125
DOI: 10.1038/emboj.2009.333
PMCID: PMC2808380

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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