The solution structures of two human IgG1 antibodies show conformational stability and accommodate their C1q and FcÎ³R ligands.
Rayner, Lucy E; Hui, Gar Kay; Gor, Jayesh; Heenan, Richard K; Dalby, Paul A; Perkins, Stephen J.
J Biol Chem
; 290(13): 8420-38, 2015 Mar 27.
Artigo em Inglês | MEDLINE | ID: mdl-25659433
Structure and Dynamics of Immunoglobulin G Glycoproteins.
Affimer proteins inhibit immune complex binding to FcÎ³RIIIa with high specificity through competitive and allosteric modes of action.
Structure of FcÎ³RI in complex with Fc reveals the importance of glycan recognition for high-affinity IgG binding.
Human IgG4: a structural perspective.
IgG Fc Glycosylation in Human Immunity.
Characterization of the NISTmAb Reference Material using small-angle scattering and molecular simulation : Part II: Concentrated protein solutions.
Disulfide Modified IgG1: An Investigation of Biophysical Profile and Clinically Relevant Fc Interactions.
Type I and type II Fc receptors regulate innate and adaptive immunity.
Molecular Basis of Assembly and Activation of Complement Component C1 in Complex with Immunoglobulin G1 and Antigen.
Explaining the non-newtonian character of aggregating monoclonal antibody solutions using small-angle neutron scattering.