3NVG

MIHFGN segment 137-142 from mouse prion

Summary for 3NVG

• Entry DOI: 10.2210/pdb3nvg/pdb
• Related: 3NVE 3NVF 3NVH
• Descriptor: Major prion protein (2 entities in total)
• Functional Keywords: amyloid-like protofibril, protein fibril
• Biological source: Mus musculus (mouse)
• Cellular location: Cell membrane; Lipid-anchor, GPI-anchor: P04925
• Total number of polymer chains: 1
• Total formula weight: 718.84

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

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

Experimental method

X-RAY DIFFRACTION (1.48 Å)