| Structural highlights
4zet is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , |
| Related: | 4zes |
| Gene: | CLEC4C, BDCA2, CLECSF11, CLECSF7, DLEC, HECL, UNQ9361/PRO34150 (HUMAN) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[CLC4C_HUMAN] Involved in antigen-capturing. Target ligand into antigen processing and peptide-loading compartments for presentation to T-cells. May mediate potent inhibition of induction of IFN-alpha/beta expression in plasmacytoid dendritic cells. May act as a signaling receptor that activates protein-tyrosine kinases and mobilizes intracellular calcium. Does not seem to bind mannose.[1] [2]
Publication Abstract from PubMed
Blood dendritic cell antigen 2 (BDCA-2; also designated CLEC4C or CD303) is uniquely expressed on plasmacytoid dendritic cells. Stimulation of BDCA-2 with antibodies leads to an anti-inflammatory response in these cells, but the natural ligands for the receptor are not known. The C-type carbohydrate-recognition domain (CRD) in the extracellular portion of BDCA-2 contains a signature motif typical of C-type animal lectins that bind mannose, glucose or GlcNAc, yet it has been reported that BDCA-2 binds selectively to galactose-terminated, bi-antennary N-linked glycans. A combination of glycan array analysis and binding competition studies with monosaccharides and natural and synthetic oligosaccharides have been used to define the binding epitope for BDCA-2 as the trisaccharides Galbeta1-3/4GlcNAcbeta1-2Man. X-ray crystallography and mutagenesis studies show that mannose is ligated to the conserved Ca2+ in the primary binding site that is characteristic of C-type CRDs, and the GlcNAc and galactose residues make additional interactions in a wide, shallow groove adjacent to the primary binding site. As predicted from these studies, BDCA-2 binds to IgG, which bears galactose-terminated glycans that are not commonly found attached to other serum glycoproteins. Thus, BDCA-2 has the potential to serve as a previously unrecognized immunoglobulin Fc receptor.
A novel mechanism for binding of galactose-terminated glycans by the C-type carbohydrate-recognition domain in blood dendritic cell antigen 2.,Jegouzo SA, Feinberg H, Dungarwalla T, Drickamer K, Weis WI, Taylor ME J Biol Chem. 2015 May 20. pii: jbc.M115.660613. PMID:25995448[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dzionek A, Sohma Y, Nagafune J, Cella M, Colonna M, Facchetti F, Gunther G, Johnston I, Lanzavecchia A, Nagasaka T, Okada T, Vermi W, Winkels G, Yamamoto T, Zysk M, Yamaguchi Y, Schmitz J. BDCA-2, a novel plasmacytoid dendritic cell-specific type II C-type lectin, mediates antigen capture and is a potent inhibitor of interferon alpha/beta induction. J Exp Med. 2001 Dec 17;194(12):1823-34. PMID:11748283
- ↑ Fernandes MJ, Iscove NN, Gingras G, Calabretta B. Identification and characterization of the gene for a novel C-type lectin (CLECSF7) that maps near the natural killer gene complex on human chromosome 12. Genomics. 2000 Oct 15;69(2):263-70. PMID:11031109 doi:http://dx.doi.org/10.1006/geno.2000.6316
- ↑ Jegouzo SA, Feinberg H, Dungarwalla T, Drickamer K, Weis WI, Taylor ME. A novel mechanism for binding of galactose-terminated glycans by the C-type carbohydrate-recognition domain in blood dendritic cell antigen 2. J Biol Chem. 2015 May 20. pii: jbc.M115.660613. PMID:25995448 doi:http://dx.doi.org/10.1074/jbc.M115.660613
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