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PDBsum entry 4tut
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Membrane protein, de novo protein
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PDB id
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4tut
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References listed in PDB file
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Key reference
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Title
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Crystal structures of polymorphic prion protein β1 peptides reveal variable steric zipper conformations.
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Authors
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L.Yu,
S.J.Lee,
V.C.Yee.
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Ref.
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Biochemistry, 2015,
54,
3640-3648.
[DOI no: ]
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PubMed id
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Abstract
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The pathogenesis of prion diseases is associated with the conformational
conversion of normal, predominantly α-helical prion protein (PrP(C)) into a
pathogenic form that is enriched with β-sheets (PrP(Sc)). Several PrP(C)
crystal structures have revealed β1-mediated intermolecular sheets, suggesting
that the β1 strand may contribute to a possible initiation site for
β-sheet-mediated PrP(Sc) propagation. This β1 strand contains the polymorphic
residue 129 that influences disease susceptibility and phenotype. To investigate
the effect of the residue 129 polymorphism on the conformation of amyloid-like
continuous β-sheets formed by β1, crystal structures of β1 peptides
containing each of the polymorphic residues were determined. To probe the
conformational influence of the peptide construct design, four different lengths
of β1 peptides were studied. From the 12 peptides studied, 11 yielded crystal
structures ranging in resolution from 0.9 to 1.4 Å. This ensemble of β1
crystal structures reveals conformational differences that are influenced by
both the nature of the polymorphic residue and the extent of the peptide
construct, indicating that comprehensive studies in which peptide constructs
vary are a more rigorous approach to surveying conformational possibilities.
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Headers
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