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2015 ; 268
(1
): 139-59
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Human IgG4: a structural perspective
#MMPMID26497518
Davies AM
; Sutton BJ
Immunol Rev
2015[Nov]; 268
(1
): 139-59
PMID26497518
show ga
IgG4, the least represented human IgG subclass in serum, is an intriguing
antibody with unique biological properties, such as the ability to undergo
Fab-arm exchange and limit immune complex formation. The lack of effector
functions, such as antibody-dependent cell-mediated cytotoxicity and
complement-dependent cytotoxicity, is desirable for therapeutic purposes. IgG4
plays a protective role in allergy by acting as a blocking antibody, and
inhibiting mast cell degranulation, but a deleterious role in malignant melanoma,
by impeding IgG1-mediated anti-tumor immunity. These findings highlight the
importance of understanding the interaction between IgG4 and Fc? receptors.
Despite a wealth of structural information for the IgG1 subclass, including
complexes with Fc? receptors, and structures for intact antibodies,
high-resolution crystal structures were not reported for IgG4-Fc until recently.
Here, we highlight some of the biological properties of human IgG4, and review
the recent crystal structures of IgG4-Fc. We discuss the unexpected conformations
adopted by functionally important C?2 domain loops, and speculate about potential
implications for the interaction between IgG4 and Fc?Rs.
|Animals
[MESH]
|Antibody Affinity/immunology
[MESH]
|Antibody Specificity/immunology
[MESH]
|Binding Sites
[MESH]
|Complement C1q/immunology/metabolism
[MESH]
|Glycosylation
[MESH]
|Humans
[MESH]
|Hypersensitivity/immunology/therapy
[MESH]
|Immunoglobulin Fab Fragments/chemistry/metabolism
[MESH]
|Immunoglobulin G/*chemistry/*immunology/metabolism/therapeutic use
[MESH]
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