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PDBsum entry 4zet
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Carbohydrate-binding protein
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PDB id
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4zet
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References listed in PDB file
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Key reference
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Title
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A novel mechanism for binding of galactose-Terminated glycans by the c-Type carbohydrate recognition domain in blood dendritic cell antigen 2.
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Authors
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S.A.Jégouzo,
H.Feinberg,
T.Dungarwalla,
K.Drickamer,
W.I.Weis,
M.E.Taylor.
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Ref.
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J Biol Chem, 2015,
290,
16759-16771.
[DOI no: ]
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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Abstract
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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 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,
biantennary 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
trisaccharide Galβ1-3/4GlcNAcβ1-2Man. X-ray crystallography and mutagenesis
studies show that mannose is ligated to the conserved Ca(2+) in the primary
binding site that is characteristic of C-type carbohydrate recognition domains,
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.
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