Abstract
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 language | English |
|---|---|
| Pages (from-to) | 54018-54022 |
| Number of pages | 5 |
| Journal | Journal of Biological Chemistry |
| Volume | 279 |
| Issue number | 52 |
| Early online date | 13 Oct 2004 |
| DOIs | |
| Publication status | Published - 24 Dec 2004 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology
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