ArticleBiophysical journal2021
Solution structure of deglycosylated human IgG1 shows the role of C
Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- 2D NMR assessment of structural consistency and functional relationships in monoclonal antibodies.mAbs · 2026Article
- Atomistic scattering modeling of the solution structure of human dimeric IgA1 reveals a structural and mechanistic basis for IgA nephropathy.The Journal of biological chemistry · 2026Article
- Article
- A Common Missense Variant, W335S, in β2-Glycoprotein I (APOH) is Associated with Increased Autoantibody Levels but Reduced Venous Thromboembolism Risk.medRxiv : the preprint server for health sciences · 2026Article
- The J-shape of β2GPI reveals a cryptic discontinuous epitope across domains I and II.Journal of structural biology: X · 2025Article
- Immunoglobulin G Subclass-Specific Glycosylation Changes in Rheumatoid Arthritis.International journal of molecular sciences · 2025Article
- Using atomistic solution scattering modelling to elucidate the role of the Fc glycans in human IgG4.PloS one · 2024Article
- The solution structure of the heavy chain-only C5-Fc nanobody reveals exposed variable regions that are optimal for COVID-19 antigen interactions.The Journal of biological chemistry · 2023Article
- Effect of Fc core fucosylation and light chain isotype on IgG1 flexibility.Communications biology · 2023Article
- Solution structures of human myeloma IgG3 antibody reveal extended Fab and Fc regions relative to the other IgG subclasses.The Journal of biological chemistry · 2021Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human immunoglobulin G (IgG) class is the most prevalent antibody in serum, with the IgG1 subclass being the most abundant. IgG1 is composed of two Fab regions connected to a Fc region through a 15-residue hinge peptide. Two glycan chains are conserved in the Fc region in IgG; however, their importance for the structure of intact IgG1 has remained unclear. Here, we subjected glycosylated and deglycosylated monoclonal human IgG1 (designated as A33) to a comparative multidisciplinary structural study of both forms. After deglycosylation using peptide:N-glycosidase F, analytical ultracentrifugation showed that IgG1 remained monomeric and the sedimentation coefficients s
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