The structural basis for the functional versatility of immunoglobulin G
- 1 December 1978
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Biochemistry
- Vol. 56 (12) , 1087-1101
- https://doi.org/10.1139/o78-172
Abstract
Current concepts of the structure of vertebrate immunoglobulin [Ig] G were reviewed. Contact residues in the antigen-combining site are contributed by the hypervariable regions of the H- and L-chains. Protein A of Staphylococcus aureus binds to IgG through a site formed by the C2 [2 chain constant region] and C3 domains of the Fc fragment.This publication has 15 references indexed in Scilit:
- Correlation between the exposure of aromatic chromophores at the surface of the Fc domains of immunoglobulin G and their ability to bind complementBiochemistry, 1977
- Immunoglobulin Binding by Mouse Intestinal Epithelial Cell ReceptorsThe Journal of Immunology, 1976
- Covalent assembly of mouse immunoglobulin G subclasses in vitro: application of a theoretical model for interchain disulfide bond formationCanadian Journal of Biochemistry, 1976
- STRUCTURE AND FUNCTION OF IMMUNOGLOBULIN DOMAINS .5. BINDING OF IMMUNOGLOBULIN-G AND FRAGMENTS TO PLACENTAL MEMBRANE PREPARATIONS1976
- Crystallographic Structural Studies of a Human Fc Fragment. II. A Complete Model Based on a Fourier Map at 3.5 Å ResolutionHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1976
- Properties of the Fc Receptor on Macrophages and MonocytesImmunological Communications, 1976
- BIOLOGIC ACTIVITIES OF AGGREGATED GAMMA-GLOBULIN .8. AGGREGATED IMMUNOGLOBULINS OF DIFFERENT CLASSES1967
- Heterogeneity in the Complementation of Polypeptide Subunits of a Purified Antibody Isolated from an Individual RabbitThe Journal of Immunology, 1966
- THE ROLE OF DISULFIDE BONDS IN THE COMPLEMENT-FIXING AND PRECIPITATING PROPERTIES OF 7S RABBIT AND SHEEP ANTIBODIESThe Journal of Experimental Medicine, 1964
- The hydrolysis of rabbit γ-globulin and antibodies with crystalline papainBiochemical Journal, 1959