Effect of hinge region state on interaction of human IgG3 with the complement system

Covalently cross-linked rod-like dimers of human myeloma IgG3 are more efficient in the inhibition of the complement system reaction than compact dimers. This correlates with an increase in the stability of CH2 domains of the immunoglobulin in the state with the rod-like hinge region.

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Bibliographic Details
Published in:Biochemistry (Moscow) 2001-12, Vol.66 (12), p.1352-1355
Main Author: Tischenko, V M
Format: Article
Language:English
Subjects:
Complement System Proteins - metabolism
Correlation analysis
Cross-Linking Reagents - metabolism
Dimerization
Humans
Immunoglobulin Fragments - chemistry
Immunoglobulin Fragments - metabolism
Immunoglobulin G - chemistry
Immunoglobulin G - metabolism
Immunoglobulins
Myeloma Proteins - metabolism
Protein Denaturation
Protein Structure, Tertiary
Staining and Labeling
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Description
Summary:Covalently cross-linked rod-like dimers of human myeloma IgG3 are more efficient in the inhibition of the complement system reaction than compact dimers. This correlates with an increase in the stability of CH2 domains of the immunoglobulin in the state with the rod-like hinge region.
ISSN:0006-2979
1608-3040
DOI:10.1023/A:1013377611449