6PQA

GAVVGG segment 119-124 from human prion

Summary for 6PQA

• Entry DOI: 10.2210/pdb6pqa/pdb
• Related: 6PQ5
• Descriptor: Major prion protein (2 entities in total)
• Functional Keywords: amyloid-like protofibril, protein fibril
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 458.51

Authors

Apostol, M.I.,Sawaya, M.R.,Eisenberg, D. (deposition date: 2019-07-08, release date: 2020-04-15, Last modification date: 2024-03-13)

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

X-RAY DIFFRACTION (1.46 Å)