ArticleThe Journal of biological chemistry2010
Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Article
- Low-frequency Raman spectra of amyloid fibrils.The Journal of chemical physics · 2025Article
- Multiscale Simulations to Discover Self-Assembled Oligopeptides: A Benchmarking Study.Journal of chemical theory and computation · 2024Article
- Preventive or promotive effects ofHeliyon · 2023Article
- Structural consequences of sequence variation in mammalian prion β2α2 loop segments.Frontiers in neuroscience · 2022Article
- In Silico Modeling of the Influence of Environment on Amyloid Folding Using FOD-M Model.International journal of molecular sciences · 2021Article
- The Three Glycotypes in the London Classification System of Sporadic Creutzfeldt-Jakob Disease Differ in Disease Duration.Molecular neurobiology · 2021Article
- Structural evidence for the critical role of the prion protein hydrophobic region in forming an infectious prion.PLoS pathogens · 2019Article
- Structural basis for the complete resistance of the human prion protein mutant G127V to prion disease.Scientific reports · 2018Article
- Towards the design of anti-amyloid short peptide helices.Bioinformation · 2018Article
- Are Amyloid Fibrils RNA-Traps? A Molecular Dynamics Perspective.Frontiers in molecular biosciences · 2018Article
- Toward the Atomic Structure of PrPCold Spring Harbor perspectives in biology · 2017Review
- Review
- N-terminal Prion Protein Peptides (PrP(120-144)) Form Parallel In-register β-Sheets via Multiple Nucleation-dependent Pathways.The Journal of biological chemistry · 2016Article
- An Atomistic View of Amyloidogenic Self-assembly: Structure and Dynamics of Heterogeneous Conformational States in the Pre-nucleation Phase.Scientific reports · 2016Article
- The Distribution of Prion Protein Allotypes Differs Between Sporadic and Iatrogenic Creutzfeldt-Jakob Disease Patients.PLoS pathogens · 2016Article
- Measurement of amyloid formation by turbidity assay-seeing through the cloud.Biophysical reviews · 2016Review
- Human prion protein sequence elements impede cross-species chronic wasting disease transmission.The Journal of clinical investigation · 2015Article
- De novo design and experimental characterization of ultrashort self-associating peptides.PLoS computational biology · 2014Article
- A proposed mechanism for the promotion of prion conversion involving a strictly conserved tyrosine residue in the β2-α2 loop of PrPC.The Journal of biological chemistry · 2014Article
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4 authors.
Funding
Abstract
A single nucleotide polymorphism (SNP) in codon 129 of the human prion gene, leading to a change from methionine to valine at residue 129 of prion protein (PrP), has been shown to be a determinant in the susceptibility to prion disease. However, the molecular basis of this effect remains unexplained. In the current study, we determined crystal structures of prion segments having either Met or Val at residue 129. These 6-residue segments of PrP centered on residue 129 are "steric zippers," pairs of interacting β-sheets. Both structures of these "homozygous steric zippers" reveal direct intermolecular interactions between Met or Val in one sheet and the identical residue in the mating sheet. These two structures, plus a structure-based model of the heterozygous Met-Val steric zipper, suggest an explanation for the previously observed effects of this locus on prion disease susceptibility and progression.
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