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- W2079576324 abstract "Atomic-level structural investigation of the key conformational intermediates of amyloidogenesis remains a challenge. Here we demonstrate the utility of nanobodies to trap and characterize intermediates of β2-microglobulin (β2m) amyloidogenesis by X-ray crystallography. For this purpose, we selected five single domain antibodies that block the fibrillogenesis of a proteolytic amyloidogenic fragment of β2m (ΔN6β2m). The crystal structure of ΔN6β2m in complex with one of these nanobodies (Nb24) identifies domain swapping as a plausible mechanism of self-association of this amyloidogenic protein. In the swapped dimer, two extended hinge loops—corresponding to the heptapetide NHVTLSQ that forms amyloid in isolation—are unmasked and fold into a new two-stranded antiparallel β-sheet. The β-strands of this sheet are prone to self-associate and stack perpendicular to the direction of the strands to build large intermolecular β-sheets that run parallel to the axis of growing oligomers, providing an elongation mechanism by self-templated growth." @default.
- W2079576324 created "2016-06-24" @default.
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- W2079576324 date "2011-01-10" @default.
- W2079576324 modified "2023-10-18" @default.
- W2079576324 title "Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic β2-microglobulin variant" @default.
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- W2079576324 doi "https://doi.org/10.1073/pnas.1008560108" @default.
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