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PDBsum entry 3nhc
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Protein fibril
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PDB id
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3nhc
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References listed in PDB file
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Key reference
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Title
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Crystallographic studies of prion protein (prp) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease.
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Authors
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M.I.Apostol,
M.R.Sawaya,
D.Cascio,
D.Eisenberg.
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Ref.
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J Biol Chem, 2010,
285,
29671-29675.
[DOI no: ]
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PubMed id
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Abstract
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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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Headers
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