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Deposition diseases and 3D domain swapping.
Melanie J Bennett1, Michael R Sawaya, David Eisenberg
1Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California 90095, USA.
3D domain swapping contributes to protein aggregation in normal cellular structures and diseases. This review examines its role in amyloid fibrils, prion proteins, and macroscopic deposits, highlighting its implication in protein deposition disorders.
Area of Science:
- Structural biology
- Biochemistry
- Molecular pathology
Background:
- Protein aggregation is fundamental to cellular function and disease.
- Structural characterization of aggregates is challenging due to limited order.
- 3D domain swapping is a proposed mechanism in protein aggregate formation.
Purpose of the Study:
- To review structures of protein aggregates formed via 3D domain swapping.
- To discuss the role of 3D domain swapping in protein deposition diseases.
Main Methods:
- Literature review of known structures.
- Analysis of protein aggregation mechanisms.
Main Results:
- 3D domain swapping is implicated in amyloid fibrils, prion proteins, and macroscopic aggregates.
- Structural insights into aggregate formation are provided.
Conclusions:
- 3D domain swapping is a significant factor in various protein aggregation phenomena.
- Understanding domain swapping is crucial for studying protein deposition diseases.
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