ArticleNature structural & molecular biology2011
β₂-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages.
Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed.
- Oligomer assembly ofToxicon: X · 2025Article
- Apoprotein Intermolecular Interactions and Heme Insertion for 3D Domain Swapping in Myoglobin.ACS omega · 2025Article
- New triple therapy for the diagnosis of CKD-MBD: a cross-sectional study in Shanxi province.BMJ open · 2024Article
- Bile acid-sensitive human norovirus strains are susceptible to sphingosine-1-phosphate receptor 2 inhibition.Journal of virology · 2024Article
- Amyloid formation and depolymerization of tumor suppressor p16Nature communications · 2024Article
- Cryo-EM structure of a human LECT2 amyloid fibril reveals a network of polar ladders at its core.Structure (London, England : 1993) · 2023Article
- Repair of DNA double-strand breaks in plant meiosis: role of eukaryotic RecA recombinases and their modulators.Plant reproduction · 2023Review
- Slow Evolution toward "Super-Aggregation" of the Oligomers Formed through the Swapping of RNase A N-Termini: A Wish for Amyloidosis?International journal of molecular sciences · 2022Article
- NOS1AP Interacts with α-Synuclein and Aggregates in Yeast and Mammalian Cells.International journal of molecular sciences · 2022Article
- Is amyloid fibrillation related to 3D domain swapping for the C-terminal domain of SARS-CoV main protease?International journal of biological macromolecules · 2022Article
- Amyloids as Building Blocks for Macroscopic Functional Materials: Designs, Applications and Challenges.International journal of molecular sciences · 2021Review
- Exploration of Insulin Amyloid Polymorphism Using Raman Spectroscopy and Imaging.Biophysical journal · 2020Article
- Cross-talk between redox signalling and protein aggregation.Biochemical Society transactions · 2020Review
- Assembly of platforms for signal transduction in the new era: dimerization, helical filament assembly, and beyond.Experimental & molecular medicine · 2020Review
- The Early Phase of β2-Microglobulin Aggregation: Perspectives From Molecular Simulations.Frontiers in molecular biosciences · 2020Review
- Article
- Biological Activities of Secretory RNases: Focus on Their Oligomerization to Design Antitumor Drugs.Frontiers in immunology · 2019Review
- Evaluation of variability in high-resolution protein structures by global distance scoring.Heliyon · 2018Article
- Towards the design of anti-amyloid short peptide helices.Bioinformation · 2018Article
- Quinary interactions with an unfolded state ensemble.Protein science : a publication of the Protein Society · 2017Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
β₂-microglobulin (β₂m) is the light chain of the type I major histocompatibility complex. It deposits as amyloid fibrils within joints during long-term hemodialysis treatment. Despite the devastating effects of dialysis-related amyloidosis, full understanding of how fibrils form from soluble β₂m remains elusive. Here we show that β₂m can oligomerize and fibrillize via three-dimensional domain swapping. Isolating a covalently bound, domain-swapped dimer from β₂m oligomers on the pathway to fibrils, we were able to determine its crystal structure. The hinge loop that connects the swapped domain to the core domain includes the fibrillizing segment LSFSKD, whose atomic structure we also determined. The LSFSKD structure reveals a class 5 steric zipper, akin to other amyloid spines. The structures of the dimer and the zipper spine fit well into an atomic model for this fibrillar form of β₂m, which assembles slowly under physiological conditions.
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