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PDBsum entry 1dqo
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Sugar binding protein
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PDB id
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1dqo
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the cysteine-Rich domain of mannose receptor complexed with a sulfated carbohydrate ligand.
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Authors
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Y.Liu,
A.J.Chirino,
Z.Misulovin,
C.Leteux,
T.Feizi,
M.C.Nussenzweig,
P.J.Bjorkman.
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Ref.
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J Exp Med, 2000,
191,
1105-1116.
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PubMed id
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Abstract
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The macrophage and epithelial cell mannose receptor (MR) binds carbohydrates on
foreign and host molecules. Two portions of MR recognize carbohydrates: tandemly
arranged C-type lectin domains facilitate carbohydrate-dependent macrophage
uptake of infectious organisms, and the NH(2)-terminal cysteine-rich domain
(Cys-MR) binds to sulfated glycoproteins including pituitary hormones. To
elucidate the mechanism of sulfated carbohydrate recognition, we determined
crystal structures of Cys-MR alone and complexed with
4-sulfated-N-acetylgalactosamine at 1.7 and 2.2 A resolution, respectively.
Cys-MR folds into an approximately three-fold symmetric beta-trefoil shape
resembling fibroblast growth factor. The sulfate portions of
4-sulfated-N-acetylgalactosamine and an unidentified ligand found in the native
crystals bind in a neutral pocket in the third lobe. We use the structures to
rationalize the carbohydrate binding specificities of Cys-MR and compare the
recognition properties of Cys-MR with other beta-trefoil proteins.
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