Solution structure of deglycosylated human IgG1 shows the role of C
Journal
Biophysical journal
ISSN: 1542-0086
Titre abrégé: Biophys J
Pays: United States
ID NLM: 0370626
Informations de publication
Date de publication:
04 05 2021
04 05 2021
Historique:
received:
17
11
2020
revised:
04
02
2021
accepted:
24
02
2021
pubmed:
7
3
2021
medline:
1
6
2021
entrez:
6
3
2021
Statut:
ppublish
Résumé
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
Identifiants
pubmed: 33675758
pii: S0006-3495(21)00196-X
doi: 10.1016/j.bpj.2021.02.038
pmc: PMC8204293
pii:
doi:
Substances chimiques
Immunoglobulin G
0
Polysaccharides
0
Receptors, IgG
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
1814-1834Informations de copyright
Copyright © 2021 Biophysical Society. Published by Elsevier Inc. All rights reserved.
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