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8FF3

Amyloid-beta (1-40) fibrils derived from familial Dutch-type CAA patient (population B)

Summary for 8FF3
Entry DOI10.2210/pdb8ff3/pdb
EMDB information29036 29037 29038
DescriptorAmyloid-beta precursor protein (1 entity in total)
Functional Keywordsamyloid, vascular, fibril, human, protein fibril
Biological sourceHomo sapiens (human)
Total number of polymer chains6
Total formula weight26015.11
Authors
Crooks, E.J.,Fu, Z.,Chowdury, S.,Smith, S.O. (deposition date: 2022-12-07, release date: 2023-12-06, Last modification date: 2024-05-01)
Primary citationFu, Z.,Crooks, E.J.,Irizarry, B.A.,Zhu, X.,Chowdhury, S.,Van Nostrand, W.E.,Smith, S.O.
An electrostatic cluster guides A beta 40 fibril formation in sporadic and Dutch-type cerebral amyloid angiopathy.
J.Struct.Biol., 216:108092-108092, 2024
Cited by
PubMed Abstract: Cerebral amyloid angiopathy (CAA) is associated with the accumulation of fibrillar Aβ peptides upon and within the cerebral vasculature, which leads to loss of vascular integrity and contributes to disease progression in Alzheimer's disease (AD). We investigate the structure of human-derived Aβ40 fibrils obtained from patients diagnosed with sporadic or familial Dutch-type (E22Q) CAA. Using cryo-EM, two primary structures are identified containing elements that have not been observed in in vitro Aβ40 fibril structures. One population has an ordered N-terminal fold comprised of two β-strands stabilized by electrostatic interactions involving D1, E22, D23 and K28. This charged cluster is disrupted in the second population, which exhibits a disordered N-terminus and is favored in fibrils derived from the familial Dutch-type CAA patient. These results illustrate differences between human-derived CAA and AD fibrils, and how familial CAA mutations can guide fibril formation.
PubMed: 38615725
DOI: 10.1016/j.jsb.2024.108092
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.09 Å)
Structure validation

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PDB entries from 2024-11-06

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