The solution structure of the human IgG2 subclass is distinct from those for human IgG1 and IgG4 providing an explanation for their discrete functions.
Hui, Gar Kay; Gardener, Antoni D; Begum, Halima; Eldrid, Charles; Thalassinos, Konstantinos; Gor, Jayesh; Perkins, Stephen J.
J Biol Chem
; 294(28): 10789-10806, 2019 Jul 12.
Artigo em Inglês | MEDLINE | ID: mdl-31088911
The Fab conformations in the solution structure of human immunoglobulin G4 (IgG4) restrict access to its Fc region: implications for functional activity.
The solution structures of two human IgG1 antibodies show conformational stability and accommodate their C1q and FcÎ³R ligands.
Masking of the Fc region in human IgG4 by constrained X-ray scattering modelling: implications for antibody function and therapy.
Analytical ultracentrifugation combined with X-ray and neutron scattering: Experiment and modelling.
Characterization of the NISTmAb Reference Material using small-angle scattering and molecular simulation : Part II: Concentrated protein solutions.
The solution structure of rabbit IgG accounts for its interactions with the Fc receptor and complement C1q and its conformational stability.
Characterization of the NISTmAb Reference Material using small-angle scattering and molecular simulation : Part I: Dilute protein solutions.
Assessment of disulfide and hinge modifications in monoclonal antibodies.
[Analysis of Antibodies with Superior Antigen-recognition in Serum from Patients Infected by Necator americanus].
The effect of a point mutation on the stability of IgG4 as monitored by analytical ultracentrifugation.