6TI5

A New Structural Model of Abeta(1-40) Fibrils

Summary for 6TI5

Entry DOI	10.2210/pdb6ti5/pdb
NMR Information	BMRB: 34454
Descriptor	Amyloid-beta precursor protein (1 entity in total)
Functional Keywords	amyloid beta peptides, alzheimer's disease, supramolecular assembly, protein fibril
Biological source	Homo sapiens (Human)
Total number of polymer chains	16
Total formula weight	69373.63
Authors	Bertini, I.,Gonnelli, L.,Luchinat, C.,Mao, J.,Nesi, A. (deposition date: 2019-11-21, release date: 2020-07-22, Last modification date: 2024-06-19)
Primary citation	Cerofolini, L.,Ravera, E.,Bologna, S.,Wiglenda, T.,Boddrich, A.,Purfurst, B.,Benilova, I.,Korsak, M.,Gallo, G.,Rizzo, D.,Gonnelli, L.,Fragai, M.,De Strooper, B.,Wanker, E.E.,Luchinat, C. Mixing A beta (1-40) and A beta (1-42) peptides generates unique amyloid fibrils. Chem.Commun.(Camb.), 56:8830-8833, 2020 Cited by PubMed Abstract: Recent structural studies show distinct morphologies for the fibrils of Aβ(1-42) and Aβ(1-40), which are believed not to co-fibrillize. We describe here a novel, structurally-uniform 1 : 1 mixed fibrillar species, which differs from both pure fibrils. It forms preferentially even when Aβ(1-42) : Aβ(1-40) peptides are mixed in a non-stoichiometric ratio. PubMed: 32749391 DOI: 10.1039/d0cc02463e PDB entries with the same primary citation
Experimental method	SOLID-STATE NMR

Structure validation