2ARB
Pterocarpus angolensis Lectin (PAL) In Complex With The GlcNAc(beta1-2)Man Disaccharide
Summary for 2ARB
Entry DOI | 10.2210/pdb2arb/pdb |
Related | 1Q8O 1S1A 2AR6 2ARE |
Descriptor | lectin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose, MANGANESE (II) ION, ... (5 entities in total) |
Functional Keywords | lectin, carbohydrate recognition, sugar binding protein |
Biological source | Pterocarpus angolensis |
Total number of polymer chains | 2 |
Total formula weight | 56107.38 |
Authors | Buts, L.,Garcia-Pino, A.,Imberty, A.,Amiot, N.,Boons, G.-J.,Versees, W.,Lah, J.,Beeckmans, S.,Wyns, L.,Loris, R. (deposition date: 2005-08-19, release date: 2006-08-01, Last modification date: 2023-08-23) |
Primary citation | Buts, L.,Garcia-Pino, A.,Imberty, A.,Amiot, N.,Boons, G.J.,Beeckmans, S.,Versees, W.,Wyns, L.,Loris, R. Structural basis for the recognition of complex-type biantennary oligosaccharides by Pterocarpus angolensis lectin. Febs J., 273:2407-2420, 2006 Cited by PubMed Abstract: The crystal structure of Pterocarpus angolensis lectin is determined in its ligand-free state, in complex with the fucosylated biantennary complex type decasaccharide NA2F, and in complex with a series of smaller oligosaccharide constituents of NA2F. These results together with thermodynamic binding data indicate that the complete oligosaccharide binding site of the lectin consists of five subsites allowing the specific recognition of the pentasaccharide GlcNAc beta(1-2)Man alpha(1-3)[GlcNAc beta(1-2)Man alpha(1-6)]Man. The mannose on the 1-6 arm occupies the monosaccharide binding site while the GlcNAc residue on this arm occupies a subsite that is almost identical to that of concanavalin A (con A). The core mannose and the GlcNAc beta(1-2)Man moiety on the 1-3 arm on the other hand occupy a series of subsites distinct from those of con A. PubMed: 16704415DOI: 10.1111/j.1742-4658.2006.05248.x PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
Download full validation report