Journal
STRUCTURE
Volume 14, Issue 5, Pages 811-824Publisher
CELL PRESS
DOI: 10.1016/j.str.2006.03.011
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Protein aggregation is a feature of both normal cellular assemblies and pathological protein depositions. Although the limited order of aggregates has often impeded their structural characterization, 3D domain swapping has been implicated in the formation of several protein aggregates. Here, we review known structures displaying 3D domain swapping in the context of amyloid and related fibrils, prion proteins, and macroscopic aggregates, and we discuss the possible involvement of domain swapping in protein deposition diseases.
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