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1UCT

Crystal structure of the extracellular fragment of Fc alpha Receptor I (CD89)

Summary for 1UCT
Entry DOI10.2210/pdb1uct/pdb
DescriptorImmunoglobulin alpha Fc receptor (2 entities in total)
Functional Keywordsbeta stands, immune system
Biological sourceHomo sapiens (human)
Cellular locationIsoform A. Isoform A. Isoform A. Isoform B: Secreted. Isoform B-delta-S2: Secreted: P24071
Total number of polymer chains1
Total formula weight25006.26
Authors
Ding, Y.,Xu, G.,Yang, M.,Zhang, W.,Rao, Z. (deposition date: 2003-04-21, release date: 2003-07-22, Last modification date: 2024-11-13)
Primary citationDing, Y.,Xu, G.,Yang, M.,Yao, M.,Gao, G.F.,Zhang, W.,Rao, Z.
Crystal Structure of the Ectodomain of Human Fc{alpha}RI.
J.Biol.Chem., 278:27966-27970, 2003
Cited by
PubMed Abstract: Human 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.
PubMed: 12783876
DOI: 10.1074/jbc.C300223200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

239149

數據於2025-07-23公開中

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