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Crystal structure of the extracellular fragment of Fc alpha Receptor I (CD89)Crystal structure of the extracellular fragment of Fc alpha Receptor I (CD89)
Structural highlights
FunctionFCAR_HUMAN Binds to the Fc region of immunoglobulins alpha. Mediates several functions including cytokine production. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHuman FcalphaRI (CD89) is the receptor specific for IgA, an immunoglobulin that is abundant in mucosa and is also found in high concentrations in serum. Although FcalphaRI is an immunoglobulin Fc receptor (FcR), it differs in many ways from FcRs for other immunoglobulin classes. The genes of most FcRs are located on chromosome 1 at 1q21-23, whereas FcalphaRI is on chromosome 19, at 19q13.4, a region called the leukocyte receptor complex, because it is clustered with several leukocyte receptor families including killer cell inhibitory receptors (KIRs) and leukocyte Ig-like receptors (LIRs). The amino acid sequence of FcalphaRI shares only 20% homology with other FcRs but it has around 35% homology with its neighboring LIRs and KIRs. In this work, we analyzed the crystal structure of the ectodomain of FcalphaRI and examined structure similarities between FcalphaRI and KIR2DL1, KIR2DL2 and LIR-1. Our data show that FcalphaRI, KIRs, and LIRs share a common hydrophobic core in their interdomain interface, and FcalphaRI is evolutionally closer to LIR than KIR. Crystal structure of the ectodomain of human FcalphaRI.,Ding Y, Xu G, Yang M, Yao M, Gao GF, Wang L, Zhang W, Rao Z J Biol Chem. 2003 Jul 25;278(30):27966-70. Epub 2003 Jun 3. PMID:12783876[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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