1dqo | pdb_00001dqo
CRYSTAL STRUCTURE OF THE CYSTEINE RICH DOMAIN OF MANNOSE RECEPTOR COMPLEXED WITH ACETYLGALACTOSAMINE-4-SULFATE
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Overview
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.
About this Structure
1DQO is a Single protein structure of sequence from Mus musculus with ASG as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the cysteine-rich domain of mannose receptor complexed with a sulfated carbohydrate ligand., Liu Y, Chirino AJ, Misulovin Z, Leteux C, Feizi T, Nussenzweig MC, Bjorkman PJ, J Exp Med. 2000 Apr 3;191(7):1105-16. PMID:10748229
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