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PDBsum entry 3vyj
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Carbohydrate binding protein
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PDB id
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3vyj
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References listed in PDB file
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Key reference
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Title
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Recognition of bisecting n-Acetylglucosamine: structural basis for asymmetric interaction with the mouse lectin dendritic cell inhibitory receptor 2.
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Authors
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M.Nagae,
K.Yamanaka,
S.Hanashima,
A.Ikeda,
K.Morita-Matsumoto,
T.Satoh,
N.Matsumoto,
K.Yamamoto,
Y.Yamaguchi.
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Ref.
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J Biol Chem, 2013,
288,
33598-33610.
[DOI no: ]
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PubMed id
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Abstract
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Dendritic cell inhibitory receptor 2 (DCIR2) is a C-type lectin expressed on
classical dendritic cells. We recently identified the unique ligand specificity
of mouse DCIR2 (mDCIR2) toward biantennary complex-type glycans containing
bisecting N-acetylglucosamine (GlcNAc). Here, we report the crystal structures
of the mDCIR2 carbohydrate recognition domain in unliganded form as well as in
complex with an agalactosylated complex-type N-glycan unit carrying a bisecting
GlcNAc residue. Bisecting GlcNAc and the α1-3 branch of the biantennary
oligosaccharide asymmetrically interact with canonical and non-canonical mDCIR2
residues. Ligand-protein interactions occur directly through
mDCIR2-characteristic amino acid residues as well as via a calcium ion and water
molecule. Our structural and biochemical data elucidate for the first time the
unique binding mode of mDCIR2 for bisecting GlcNAc-containing glycans, a mode
that contrasts sharply with that of other immune C-type lectin receptors such as
DC-SIGN.
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