Help Privacy Policy Disclaimer
  Advanced SearchBrowse




Journal Article

X-ray crystallographic studies of IgG-Fc gamma receptor interactions


Sondermann,  P.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available

Sondermann, P., & Oosthuizen, V. (2002). X-ray crystallographic studies of IgG-Fc gamma receptor interactions. Biochemical Society Transactions, 30, 481-486.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-6E90-A
Human Fcgamma receptors (FcgammaRs) for the Fc portion of IgG are major mediators of the adaptive immune response. Crystal structures of their extracellular domains were recently solved and shown to obey a common fold, resulting in a heart-shaped structure. Together with the multifunctional Fc fragment, whose structure was deciphered in the 1970s, the complex of an FcgammaR with Fc was recently crystallized. Its crystal structure indicates that despite the dimeric character of the Fc fragment, only one FcgammaR can bind to Fc, due to an introduced asymmetry within the homodimeric Fc, as well as by binding to symmetrically related residues of both Fc chains. Homology modelling suggested that the other FcgammaRs bind the Fc in a similar manner. The resolved complex structure can be regarded as a paradigm for Ig binding to Fc receptors and serves as a solid base for the design of compounds interfering with complex formation. Such molecules would be of invaluable benefit for the therapy of immunological disorders.