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1LOG

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

Summary for 1LOG
Entry DOI10.2210/pdb1log/pdb
DescriptorLEGUME ISOLECTIN I (ALPHA CHAIN), LEGUME ISOLECTIN I (BETA CHAIN), alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
Functional Keywordslectin
Biological sourceLathyrus ochrus (yellow-flowered pea)
More
Total number of polymer chains4
Total formula weight52543.37
Authors
Bourne, Y.,Cambillau, C. (deposition date: 1994-01-27, release date: 1994-04-30, Last modification date: 2024-02-14)
Primary citationBourne, Y.,Rouge, P.,Cambillau, C.
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.
J.Biol.Chem., 265:18161-18165, 1990
Cited by
PubMed Abstract: 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 Pérez, 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.
PubMed: 2211692
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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