Solution structures of human myeloma IgG3 antibody reveal extended Fab and Fc regions relative to the other IgG subclasses.
Amino Acid Sequence
Chromatography, Liquid
/ methods
Glycosylation
Humans
Immunoglobulin Fab Fragments
/ chemistry
Immunoglobulin G
/ chemistry
Mass Spectrometry
/ methods
Molecular Dynamics Simulation
Multiple Myeloma
/ immunology
Myeloma Proteins
/ chemistry
Neutrons
Protein Conformation
Receptors, Fc
/ chemistry
Scattering, Small Angle
Sequence Homology, Amino Acid
Ultracentrifugation
/ methods
X-Ray Diffraction
analytical ultracentrifugation
antibody modeling
human IgG subclasses
small angle X-ray scattering
small-angle neutron scattering
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
09 2021
09 2021
Historique:
received:
03
05
2021
revised:
08
07
2021
accepted:
19
07
2021
pubmed:
25
7
2021
medline:
23
11
2021
entrez:
24
7
2021
Statut:
ppublish
Résumé
Human immunoglobulin G subclass 3 (IgG3) possesses a uniquely long hinge region that separates its Fab antigen-binding and Fc receptor-binding regions. Owing to this hinge length, the molecular structure of full-length IgG3 remains elusive, and the role of the two conserved Fc glycosylation sites are unknown. To address these issues, we subjected glycosylated and deglycosylated human myeloma IgG3 to multidisciplinary solution structure studies. Using analytical ultracentrifugation, the elongated structure of IgG3 was determined from the reduced sedimentation coefficients s
Identifiants
pubmed: 34302810
pii: S0021-9258(21)00797-3
doi: 10.1016/j.jbc.2021.100995
pmc: PMC8371214
pii:
doi:
Substances chimiques
Immunoglobulin Fab Fragments
0
Immunoglobulin G
0
Myeloma Proteins
0
Receptors, Fc
0
myeloma immunoglobulins
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
100995Informations de copyright
Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.
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