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3NHD

GYVLGS segment 127-132 from human prion with V129

Summary for 3NHD
Entry DOI10.2210/pdb3nhd/pdb
Related3NHC
DescriptorMajor prion protein, ACETIC ACID (3 entities in total)
Functional Keywordsamyloid-like protofibril, protein fibril
Biological sourceHomo sapiens (human)
Cellular locationCell membrane; Lipid-anchor, GPI-anchor. Isoform 2: Cytoplasm: P04156
Total number of polymer chains2
Total formula weight1309.42
Authors
Apostol, M.I.,Eisenberg, D. (deposition date: 2010-06-14, release date: 2010-08-04, Last modification date: 2024-05-22)
Primary citationApostol, M.I.,Sawaya, M.R.,Cascio, D.,Eisenberg, D.
Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease.
J.Biol.Chem., 285:29671-29675, 2010
Cited by
PubMed 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.
PubMed: 20685658
DOI: 10.1074/jbc.C110.158303
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.92 Å)
Structure validation

226707

건을2024-10-30부터공개중

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