1log

From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models 1log, resolution 2.1Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

X-RAY STRUCTURE OF A (ALPHA-MAN(1-3)BETA-MAN(1-4)GLCNAC)-LECTIN COMPLEX AT 2.1 ANGSTROMS RESOLUTION

Overview

We describe herein the high resolution refined x-ray structure of a, trisaccharide, which is a part of the N-acetyllactosamine type glycan, found in the majority of the N-glycosyl-proteins, complexed to the, isolectin I. According to the potentials used by Imberty et al. (Imburty, A., Gerber, S., Tran, V., and Perez, S. (1990) Glycoconjugate J. 7, 27-54), the trisaccharide is in a low-energy state. Only one mannose moiety, establishes direct hydrogen bonds with the lectin, as it is the case for, monosaccharide-lectin complexes. The comparison of our trisaccharide with, the one determined in solution by Warin et al. (Warin, V., Baert, F., Fouret, R., Strecker, G., Fournet, B., and Montreuil, J. (1979) Carbohydr., Res. 76, 11-22) shows that both adopt roughly the same conformation. The, differences in these two sugar structures allow us to assign the role of, water molecules present in the vicinity of our trisaccharide for the, stabilization of this sugar-lectin complex.

About this Structure

1LOG is a Protein complex structure of sequences from Lathyrus ochrus with CA and MN as ligands. Full crystallographic information is available from OCA.

Reference

X-ray structure of a (alpha-Man(1-3)beta-Man(1-4)GlcNAc)-lectin complex at 2.1-A resolution. The role of water in sugar-lectin interaction., Bourne Y, Rouge P, Cambillau C, J Biol Chem. 1990 Oct 25;265(30):18161-5. PMID:2211692

Page seeded by OCA on Tue Nov 20 20:43:25 2007