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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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PDB id:
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| Name: |
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Carbohydrate-binding protein
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Title:
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Blood dendritic cell antigen 2 (bdca-2) complexed with galglcnacman
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Structure:
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C-type lectin domain family 4 member c. Chain: a, b. Fragment: unp residues 67-213. Synonym: blood dendritic cell antigen 2,bdca-2,c-type lectin superfamily member 7,dendritic lectin. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: clec4c, bdca2, clecsf11, clecsf7, dlec, hecl, unq9361/pro34150. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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2.90Å
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R-factor:
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0.182
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R-free:
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0.263
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Authors:
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S.A.F.Jegouzo,H.Feinberg,T.Dungarwalla,K.Drickamer,W.I.Weis, M.E.Taylor
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Key ref:
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S.A.Jégouzo
et al.
(2015).
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,
290,
16759-16771.
PubMed id:
DOI:
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Date:
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20-Apr-15
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Release date:
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27-May-15
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PROCHECK
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Headers
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References
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Q8WTT0
(CLC4C_HUMAN) -
C-type lectin domain family 4 member C from Homo sapiens
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Seq:
Struc:
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213 a.a.
147 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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DOI no:
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J Biol Chem
290:16759-16771
(2015)
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PubMed id:
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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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S.A.Jégouzo,
H.Feinberg,
T.Dungarwalla,
K.Drickamer,
W.I.Weis,
M.E.Taylor.
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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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Links
