7RL4

Cryo-EM structure of human PrP23-144 amyloid fibrils

Summary for 7RL4

Entry DOI	10.2210/pdb7rl4/pdb
EMDB information	24514
Descriptor	Major prion protein (1 entity in total)
Functional Keywords	prion, amyloid, protein fibril
Biological source	Homo sapiens (Human)
Total number of polymer chains	20
Total formula weight	250834.86
Authors	Li, Q.,Surewicz, W.K. (deposition date: 2021-07-23, release date: 2022-07-27, Last modification date: 2024-06-05)
Primary citation	Li, Q.,Jaroniec, C.P.,Surewicz, W.K. Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers. Nat.Struct.Mol.Biol., 29:962-965, 2022 Cited by PubMed Abstract: One of the least understood aspects of prion diseases is the structure of infectious prion protein aggregates. Here we report a high-resolution cryo-EM structure of amyloid fibrils formed by human prion protein with the Y145Stop mutation that is associated with a familial prion disease. This structural insight allows us not only to explain previous biochemical findings, but also provides direct support for the conformational adaptability model of prion transmissibility barriers. PubMed: 36097290 DOI: 10.1038/s41594-022-00833-4 PDB entries with the same primary citation
Experimental method	ELECTRON MICROSCOPY (2.86 Å)

Structure validation