Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Avian IgY is closely related to an ancestor of both mammalian IgG and IgE and thus provides insights into the evolution of antibody structure and function. A recombinant fragment of IgY-Fc consisting of a dimer of the Cupsilon3 and Cupsilon4 domains, Fcupsilon3-4, was expressed and crystallized and its X-ray structure determined to 1.75 A resolution. Fcupsilon3-4 is the only nonmammalian Fc fragment structure determined to date and provides the first structural evidence for an ancient origin of antibody architecture. The Fcupsilon3-4 structure reveals features common to both IgE-Fc and IgG-Fc, and the implications for IgY binding to its receptor are discussed.
The Crystal Structure of an Avian IgY-Fc Fragment Reveals Conservation with both Mammalian IgG and IgE (dagger) (double dagger).,Taylor AI, Fabiane SM, Sutton BJ, Calvert RA Biochemistry. 2008 Dec 30. PMID:19115948[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Taylor AI, Fabiane SM, Sutton BJ, Calvert RA. The Crystal Structure of an Avian IgY-Fc Fragment Reveals Conservation with both Mammalian IgG and IgE (dagger) (double dagger). Biochemistry. 2008 Dec 30. PMID:19115948 doi:10.1021/bi8019993
