Effect of hinge region state on interaction of human IgG3 with the complement system.
Covalently cross-linked rod-like dimers of human myeloma IgG3 are more efficient in the inhibition of the complement system reaction than compact dimers. This correlates with an increase in the stability of CH2 domains of the immunoglobulin in the state with the rod-like hinge region.
Tischenko
V M
VM
Institute of Biological Instrumentation, Russian Academy of Sciences, Pushchino, Moscow Region, 142292 Russia. tischen@vega.protres.ru
D003165:Complement System Proteins / Q000378:metabolism*; D003432:Cross-Linking Reagents / Q000378:metabolism; D019281:Dimerization; D006801:Humans; D007128:Immunoglobulin Fragments / Q000737:chemistry / Q000378:metabolism*; D007074:Immunoglobulin G / Q000737:chemistry / Q000378:metabolism*; D009194:Myeloma Proteins / Q000378:metabolism; D011489:Protein Denaturation; D017434:Protein Structure, Tertiary; D013194:Staining and Labeling
D003432:Cross-Linking Reagents; D007128:Immunoglobulin Fragments; D007074:Immunoglobulin G; D009194:Myeloma Proteins; D003165:Complement System Proteins