Structural basis for the recognition of complex-type biantennary oligosaccharides by Pterocarpus angolensis lectin.
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.
Buts
Lieven
L
Laboratorium voor Ultrastructuur, Vrije Universiteit Brussel and Department of Molecular and Cellular Interactions, Vlaams Interuniversitair Instituut voor Biotechnologie, Belgium.
Garcia-Pino
Abel
A
Imberty
Anne
A
Amiot
Nicolas
N
Boons
Geert-Jan
GJ
Beeckmans
Sonia
S
Versées
Wim
W
Wyns
Lode
L
Loris
Remy
R
D001665:Binding Sites; D002236:Carbohydrate Conformation; D004187:Disaccharides / Q000737:chemistry; D005656:Fungal Proteins / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000737:chemistry*; D037121:Plant Lectins / Q000737:chemistry*; D035721:Pterocarpus; D014312:Trisaccharides / Q000737:chemistry
D004187:Disaccharides; D005656:Fungal Proteins; D009844:Oligosaccharides; D037121:Plant Lectins; D014312:Trisaccharides