Residue at position 331 in the IgG1 and IgG4 CH2 domains contributes to their differential ability to bind and activate complement.
Open Access
- 1 February 1994
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 269 (5) , 3469-3474
- https://doi.org/10.1016/s0021-9258(17)41886-2
Abstract
No abstract availableKeywords
This publication has 34 references indexed in Scilit:
- Solution structure of human and mouse immunoglobulin M by synchrotron X-ray scattering and molecular graphics modellingJournal of Molecular Biology, 1991
- Chimeric mouse human IgG3 antibodies with an IgG4-like hinge region induce complement-mediated lysis more efficiently than IgG3 with normal hingEuropean Journal of Immunology, 1991
- Enhancement of Complement Activation and Cytolysis of Human IgG3 by Deletion of Hinge ExonsScandinavian Journal of Immunology, 1990
- Proton nuclear magnetic resonance studies of the structure of the Fc fragment of human immunoglobulin G1: Comparisons of native and recombinant proteinsMolecular Immunology, 1990
- Complement activation by immunoglobulin does not depend solely on C1q bindingEuropean Journal of Immunology, 1990
- C1q binding to chimeric monoclonal IgG3 antibodies consisting of mouse variable regions and human constant regions with shortened hinge containing 15 to 47 amino acidsEuropean Journal of Immunology, 1989
- Human monoclonal IgG isotypes differ in complement activating function at the level of C4 as well as C1q.The Journal of Experimental Medicine, 1988
- Comparison of the effector functions of human immunoglobulins using a matched set of chimeric antibodies.The Journal of Experimental Medicine, 1987
- Preparation and biologic characterization of fragments containing dimeric and monomeric Cγ2 domain of rabbit IgGMolecular Immunology, 1985
- Solvent-Accessible Surfaces of Proteins and Nucleic AcidsScience, 1983