3NVF
IIHFGS segment 138-143 from human prion
Summary for 3NVF
Entry DOI | 10.2210/pdb3nvf/pdb |
Related | 3NVE 3NVG 3NVH |
Descriptor | Major prion protein, (4S)-2-METHYL-2,4-PENTANEDIOL (2 entities in total) |
Functional Keywords | amyloid-like protofibril, protein fibril |
Biological source | Homo sapiens (human) |
Cellular location | Cell membrane; Lipid-anchor, GPI-anchor. Isoform 2: Cytoplasm: P04156 |
Total number of polymer chains | 1 |
Total formula weight | 791.95 |
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 citation | Apostol, 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: 21323366DOI: 10.1021/bi101803k PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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