6UUR

Human prion protein fibril, M129 variant

Summary for 6UUR

• Entry DOI: 10.2210/pdb6uur/pdb
• EMDB information: 20900
• Descriptor: Major prion protein (1 entity in total)
• Functional Keywords: amyloid, fibril, prion, filament, protein fibril, fiber, prp
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 10
• Total formula weight: 96857.71

Authors

Glynn, C.,Sawaya, M.R.,Ge, P.,Zhou, Z.H.,Rodriguez, J.A. (deposition date: 2019-10-31, release date: 2020-04-15, Last modification date: 2025-05-21)

Primary citation

Glynn, C.,Sawaya, M.R.,Ge, P.,Gallagher-Jones, M.,Short, C.W.,Bowman, R.,Apostol, M.,Zhou, Z.H.,Eisenberg, D.S.,Rodriguez, J.A.
Cryo-EM structure of a human prion fibril with a hydrophobic, protease-resistant core.
Nat.Struct.Mol.Biol., 27:417-423, 2020

PubMed Abstract: Self-templating assemblies of the human prion protein are clinically associated with transmissible spongiform encephalopathies. Here we present the cryo-EM structure of a denaturant- and protease-resistant fibril formed in vitro spontaneously by a 9.7-kDa unglycosylated fragment of the human prion protein. This human prion fibril contains two protofilaments intertwined with screw symmetry and linked by a tightly packed hydrophobic interface. Each protofilament consists of an extended beta arch formed by residues 106 to 145 of the prion protein, a hydrophobic and highly fibrillogenic disease-associated segment. Such structures of prion polymorphs serve as blueprints on which to evaluate the potential impact of sequence variants on prion disease.

PubMed: 32284600
DOI: 10.1038/s41594-020-0403-y

Experimental method

ELECTRON MICROSCOPY (3.5 Å)