Article
Structural requirements for the interaction of human IgM and IgA with the human Fcalpha/mu receptor.
European journal of immunology - 1 Apr 2009
Ghumra Ashfaq, Shi Jianguo, Mcintosh Richard S, Rasmussen Ingunn B, Braathen Ranveig, Johansen Finn-Eirik, Sandlie Inger, Mongini Patricia K, Areschoug Thomas, Lindahl Gunnar, Lewis Melanie J, Woof Jenny M, Pleass Richard J
Abstract excerpt
Here we unravel the structural features of human IgM and IgA that govern their interaction with the human Fcalpha/mu receptor (hFcalpha/muR). Ligand polymerization status was crucial for the interaction, because hFcalpha/muR binding did not occur with monomeric Ab of either class. hFcalpha/muR bound IgM with an affinity in the nanomolar range, whereas the affinity for dimeric IgA (dIgA) was tenfold lower. Panels...
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