1dqg

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1dqg, resolution 1.7Å

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CRYSTAL STRUCTURE OF THE CYSTEINE RICH DOMAIN OF MANNOSE RECEPTOR

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

1DQG is a Single protein structure of sequence from Mus musculus with SO4 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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