ArticleProceedings of the National Academy of Sciences of the United States of America2011
Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic beta2-microglobulin variant.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 118 citations in OpenAlex.
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- Targeted Protein Modification with an Antibody-Based System.ACS central science · 2025Article
- Affibodies as valuable tool to prevent βBiology direct · 2025Article
- Nanobody-based conjugates targeting small molecule-binding GPCRs and exhibiting logic-gated signaling.bioRxiv : the preprint server for biology · 2025Article
- The Impact of Nanobodies on G Protein-Coupled Receptor Structural Biology and Their Potential as Therapeutic Agents.Molecular pharmacology · 2024Review
- Structural and thermodynamic insights into antibody light chain tetramer formation through 3D domain swapping.Nature communications · 2023Article
- Structure and function of the EA1 surface layer of Bacillus anthracis.Nature communications · 2023Article
- Bypassing the Need for Cell Permeabilization: Nanobody CDR3 Peptide Improves Binding on Living Bacteria.Bioconjugate chemistry · 2023Article
- Design of Beta-2 Microglobulin Adsorbent Protein Nanoparticles.Biomolecules · 2023Article
- Design of Oscillatory Networks through Post-Translational Control of Network Components.Synthetic biology and engineering · 2023Article
- A comprehensive comparison between camelid nanobodies and single chain variable fragments.Biomarker research · 2021Review
- Activation of a G protein-coupled receptor through indirect antibody-mediated tethering of ligands.RSC chemical biology · 2021Article
- Structure of Nanobody Nb23.Molecules (Basel, Switzerland) · 2021Article
- A platform for post-translational spatiotemporal control of cellular proteins.Synthetic biology (Oxford, England) · 2021Article
- Visualizing and trapping transient oligomers in amyloid assembly pathways.Biophysical chemistry · 2021Review
- Modulation of Amyloidogenic Protein Self-Assembly Using Tethered Small Molecules.Journal of the American Chemical Society · 2020Article
- Exploring cellular biochemistry with nanobodies.The Journal of biological chemistry · 2020Review
- The Early Phase of β2-Microglobulin Aggregation: Perspectives From Molecular Simulations.Frontiers in molecular biosciences · 2020Review
- Antibody Structure and Function: The Basis for Engineering Therapeutics.Antibodies (Basel, Switzerland) · 2019Review
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Atomic-level structural investigation of the key conformational intermediates of amyloidogenesis remains a challenge. Here we demonstrate the utility of nanobodies to trap and characterize intermediates of β2-microglobulin (β2m) amyloidogenesis by X-ray crystallography. For this purpose, we selected five single domain antibodies that block the fibrillogenesis of a proteolytic amyloidogenic fragment of β2m (ΔN6β2m). The crystal structure of ΔN6β2m in complex with one of these nanobodies (Nb24) identifies domain swapping as a plausible mechanism of self-association of this amyloidogenic protein. In the swapped dimer, two extended hinge loops--corresponding to the heptapetide NHVTLSQ that forms amyloid in isolation--are unmasked and fold into a new two-stranded antiparallel β-sheet. The β-strands of this sheet are prone to self-associate and stack perpendicular to the direction of the strands to build large intermolecular β-sheets that run parallel to the axis of growing oligomers, providing an elongation mechanism by self-templated growth.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.