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PDBsum entry 3wsr
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Sugar binding protein
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PDB id
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3wsr
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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 platform of c-Type lectin-Like receptor clec-2 for binding o-Glycosylated podoplanin and nonglycosylated rhodocytin.
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Authors
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M.Nagae,
K.Morita-Matsumoto,
M.Kato,
M.K.Kaneko,
Y.Kato,
Y.Yamaguchi.
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Ref.
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Structure, 2014,
22,
1711-1721.
[DOI no: ]
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PubMed id
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Abstract
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Podoplanin is a transmembrane O-glycoprotein that binds to C-type lectin-like
receptor 2 (CLEC-2). The O-glycan-dependent interaction seems to play crucial
roles in various biological processes, such as platelet aggregation. Rhodocytin,
a snake venom, also binds to CLEC-2 and aggregates platelets in a
glycan-independent manner. To elucidate the structural basis of the
glycan-dependent and independent interactions, we performed comparative
crystallographic studies of podoplanin and rhodocytin in complex with CLEC-2.
Both podoplanin and rhodocytin bind to the noncanonical "side" face of
CLEC-2. There is a common interaction mode between consecutive acidic residues
on the ligands and the same arginine residues on CLEC-2. Other interactions are
ligand-specific. Carboxyl groups from the sialic acid residue on podoplanin and
from the C terminus of the rhodocytin α subunit interact differently at this
"second" binding site on CLEC-2. The unique and versatile binding
modes open a way to understand the functional consequences of CLEC-2-ligand
interactions.
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