4uso | pdb_00004uso

X-ray structure of the CCL2 lectin in complex with sialyl lewis X

spinqualitylabelsall models 4uso, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4uso is a 4 chain structure with sequence from Coprinopsis cinerea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.95Å Ligands: FUC, GAL, NAG, PRD_900121, SIA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B3GA02_COPCI Publication Abstract from PubMed Lectins are used as defense effector proteins against predators, parasites and pathogens by animal, plant and fungal innate defense systems. These proteins bind to specific glycoepitopes on the cell surfaces and thereby interfere with the proper cellular functions of the various antagonists. The exact cellular toxicity mechanism is in many cases unclear. Lectin CCL2 of the mushroom Coprinopsis cinerea was previously shown to be toxic for Caenorhabditis elegans and Drosophila melanogaster This toxicity is dependent on a single, high-affinity binding site for the trisaccharide GlcNAc(Fucalpha1,3)beta1,4GlcNAc, which is a hallmark of nematode and insect N-glycan cores. The carbohydrate-binding site is located at an unusual position on the protein surface when compared to other beta-trefoil lectins. Here, we show that CCL2 forms a compact dimer in solution and in crystals. Substitution of two amino acid residues at the dimer interface, R18A and F133A, interfered with dimerization of CCL2 and reduced toxicity but left carbohydrate-binding unaffected. These results, together with the positioning of the two carbohydrate-binding sites on the surface of the protein dimer, suggest that crosslinking of N-glycoproteins on the surface of intestinal cells of invertebrates is a crucial step in the mechanism of CCL2-mediated toxicity. Comparisons of the number and positioning of carbohydrate-binding sites among different dimerizing fungal beta-trefoil lectins revealed a considerable variability in the carbohydrate-binding patterns of these proteins, which are likely to correlate with their respective functions. Dimerization of the fungal defense lectin CCL2 is essential for its toxicity against nematodes.,Bleuler-Martinez S, Stutz K, Sieber R, Collot M, Mallet JM, Hengartner M, Schubert M, Varrot A, Kunzler M Glycobiology. 2016 Nov 22. PMID:27980000 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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