1DQO

Crystal structure of the cysteine rich domain of mannose receptor complexed with Acetylgalactosamine-4-sulfate

Summary for 1DQO

• Entry DOI: 10.2210/pdb1dqo/pdb
• Related: 1DQG
• Descriptor: MANNOSE RECEPTOR, 2-acetamido-2-deoxy-4-O-sulfo-beta-D-galactopyranose (3 entities in total)
• Functional Keywords: beta trefoil, multilectin receptor, pituitary hormones, sulfated carbohydrate, sugar binding protein
• Biological source: Mus musculus (house mouse)
• Cellular location: Endosome membrane; Single-pass type I membrane protein (By similarity): Q61830
• Total number of polymer chains: 1
• Total formula weight: 15859.76

Authors

Liu, Y.,Chirino, A.J.,Misulovin, Z.,Leteux, C.,Feizi, T.,Nussenzweig, M.C.,Bjorkman, P.J. (deposition date: 2000-01-04, release date: 2000-05-10, Last modification date: 2024-11-13)

Primary citation

Liu, Y.,Chirino, A.J.,Misulovin, Z.,Leteux, C.,Feizi, T.,Nussenzweig, M.C.,Bjorkman, P.J.
Crystal structure of the cysteine-rich domain of mannose receptor complexed with a sulfated carbohydrate ligand.
J.Exp.Med., 191:1105-1116, 2000

PubMed Abstract: 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.

PubMed: 10748229
DOI: 10.1084/jem.191.7.1105

Experimental method

X-RAY DIFFRACTION (2.2 Å)