| Literature DB >> 16698543 |
Melanie J Bennett1, Michael R Sawaya, David Eisenberg.
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.Entities:
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Year: 2006 PMID： 16698543 DOI： 10.1016/j.str.2006.03.011
Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006