The solution structure of the human IgG2 subclass is distinct from those for human IgG1 and IgG4 providing an explanation for their discrete functions.
Carrier Proteins
/ chemistry
Humans
Immunoglobulin Fab Fragments
/ chemistry
Immunoglobulin Fc Fragments
/ chemistry
Immunoglobulin G
/ chemistry
Models, Molecular
Molecular Structure
Neutron Diffraction
/ methods
Neutrons
Protein Binding
/ physiology
Protein Conformation
Scattering, Small Angle
Ultracentrifugation
/ methods
X-Ray Diffraction
/ methods
X-Rays
analytical ultracentrifugation
antibody
immunoglobulin G (IgG)
molecular modeling
neutron-scattering
small-angle X-ray scattering (SAXS)
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:
12 07 2019
12 07 2019
Historique:
received:
12
12
2018
revised:
03
05
2019
pubmed:
16
5
2019
medline:
4
3
2020
entrez:
16
5
2019
Statut:
ppublish
Résumé
Human IgG2 antibody displays distinct therapeutically-useful properties compared with the IgG1, IgG3, and IgG4 antibody subclasses. IgG2 is the second most abundant IgG subclass, being able to bind human FcγRII/FcγRIII but not to FcγRI or complement C1q. Structural information on IgG2 is limited by the absence of a full-length crystal structure for this. To this end, we determined the solution structure of human myeloma IgG2 by atomistic X-ray and neutron-scattering modeling. Analytical ultracentrifugation disclosed that IgG2 is monomeric with a sedimentation coefficient (
Identifiants
pubmed: 31088911
pii: S0021-9258(20)30183-6
doi: 10.1074/jbc.RA118.007134
pmc: PMC6635440
pii:
doi:
Substances chimiques
Carrier Proteins
0
Immunoglobulin Fab Fragments
0
Immunoglobulin Fc Fragments
0
Immunoglobulin G
0
prolactin-binding protein
0
Banques de données
PDB
['1HZH', '5DK3', '1IGT', '6FCZ', '4X4M', '3SGJ', '5VU0', '5YC5', '3KYM', '4HAF']
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
10789-10806Informations de copyright
© 2019 Hui et al.
Déclaration de conflit d'intérêts
The authors declare that they have no conflicts of interest with the contents of this article.
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