3lly

Crystal Structure Analysis of Maclura pomifera agglutinin

spinqualitylabelsall models 3lly, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3lly is a 2 chain structure with sequence from Maclura pomifera. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3llz, 3lm1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [LECA_MACPO] D-galactose-specific lectin, binds the T-antigen structure Gal-beta1,3-GalNAc. [LECB2_MACPO] D-galactose-specific lectin, binds the T-antigen structure Gal-beta1,3-GalNAc. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The Maclura pomifera agglutinin (MPA) recognizes the T-antigen disaccharide Galbeta1,3GalNAc mainly through interaction of the alpha-GalNAc moiety with its primary site, but the interactions of the two flanking subsites A and B with aglycones and substituents other than Gal, respectively, are not well understood. We therefore characterized the specificity of MPA in more detail by glycan micro-array analysis and determined the crystal structures of MPA without ligand and in complexes with Galbeta1,3GalNAc and p-nitrophenyl alpha-GalNAc. In both sugar complexes, pairs of ligands created inter-tetramer hydrogen-bond bridging networks. While subsite A showed increased affinity for hydrophobic aglycones, it also accommodated several sugar substituents. Notably, a GalNAc-O-tripeptide, a Tn antigen mimic, showed lower affinity than these compounds in surface plasmon resonance experiments. The glycan array data showed subsite B accepted compounds in which the O3 position of the GalNAc was substituted with various sugars other than Gal, but substitutions at O6 led to inactivity. Additions to the Gal moiety of the disaccharide also had only small effects on reactivity. These results are all compatible with the features seen in the crystal structures. Characterization of the secondary binding sites of Maclura pomifera agglutinin by glycan array and crystallographic analyses.,Huang J, Xu Z, Wang D, Ogata CM, Palczewski K, Lee X, Young NM Glycobiology. 2010 Sep 8. PMID:20826825 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Agglutinin

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