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3NVF

IIHFGS segment 138-143 from human prion

Summary for 3NVF
Entry DOI10.2210/pdb3nvf/pdb
Related3NVE 3NVG 3NVH
DescriptorMajor prion protein, (4S)-2-METHYL-2,4-PENTANEDIOL (2 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 chains1
Total formula weight791.95
Authors
Apostol, M.I.,Sawaya, M.R.,Eisenberg, D. (deposition date: 2010-07-08, release date: 2011-03-02, Last modification date: 2024-02-21)
Primary citationApostol, M.I.,Wiltzius, J.J.,Sawaya, M.R.,Cascio, D.,Eisenberg, D.
Atomic structures suggest determinants of transmission barriers in Mammalian prion disease.
Biochemistry, 50:2456-2463, 2011
Cited by
PubMed Abstract: Prion represents a unique class of pathogens devoid of nucleic acid. The deadly diseases transmitted by it between members of one species and, in certain instances, to members of other species present a public health concern. Transmissibility and the barriers to transmission between species have been suggested to arise from the degree to which a pathological protein conformation from an individual of one species can seed a pathological conformation in another species. However, this hypothesis has never been illustrated at an atomic level. Here we present three X-ray atomic structures of the same segment from human, mouse, and hamster PrP, which is critical for forming amyloid and confers species specificity in PrP seeding experiments. The structures reveal that different sequences encode different steric zippers and suggest that the degree of dissimilarity of these zipper structures gives rise to transmission barriers in prion disease, such as those that protect humans from acquiring bovine spongiform encephalopathy (BSE) and chronic wasting disease (CWD).
PubMed: 21323366
DOI: 10.1021/bi101803k
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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