title: Deposition diseases and 3D domain swapping.
abstract: 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.
authors.affiliation: Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California 90095, USA.
authors.forename: Melanie J
authors.initials: MJ
authors.lastname: Bennett
authors.forename: Michael R
authors.initials: MR
authors.lastname: Sawaya
authors.forename: David
authors.initials: D
authors.lastname: Eisenberg
mesh_terms: D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism*; D000686:Amyloidosis / Q000378:metabolism*; D003461:Crystallography; D006801:Humans; D008659:Metabolic Diseases / Q000378:metabolism*; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D000682:Amyloid