Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2ARB

Pterocarpus angolensis Lectin (PAL) In Complex With The GlcNAc(beta1-2)Man Disaccharide

Summary for 2ARB
Entry DOI10.2210/pdb2arb/pdb
Related1Q8O 1S1A 2AR6 2ARE
Descriptorlectin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose, MANGANESE (II) ION, ... (5 entities in total)
Functional Keywordslectin, carbohydrate recognition, sugar binding protein
Biological sourcePterocarpus angolensis
Total number of polymer chains2
Total formula weight56107.38
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 citationButs, 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: 16704415
DOI: 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

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon