Characterization of the ligand binding site of the bovine IgA Fc receptor (bFcαR)

H. Craig Morton, Richard J. Pleass, Jenny M. Woof, Per Brandtzaeg

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4 Citations (Scopus)
93 Downloads (Pure)


Recently, we identified a bovine IgA Fc receptor (bFcαR), which shows high homology to the human myeloid FcαR, CD89. IgA binding has previously been shown to depend on several specific residues located in the B-C and F-G loops of the membrane-distal extracellular domain 1 of CD89. To compare the ligand binding properties of these two FcαRs, we have mapped the IgA binding site of bFcαR. We show that, in common with CD89, Tyr-35 in the B-C loop is essential for IgA binding. However, in contrast to earlier observations on CD89, mutation of residues in the F-G loop did not significantly inhibit IgA binding.

Original languageEnglish
Pages (from-to)54018-54022
Number of pages5
JournalJournal of Biological Chemistry
Issue number52
Early online date13 Oct 2004
Publication statusPublished - 24 Dec 2004

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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