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

1LOF

X-RAY STRUCTURE OF A BIANTENNARY OCTASACCHARIDE-LECTIN COMPLEX AT 2.3 ANGSTROMS RESOLUTION

Summary for 1LOF
Entry DOI10.2210/pdb1lof/pdb
DescriptorLEGUME ISOLECTIN I (ALPHA CHAIN), LEGUME ISOLECTIN I (BETA CHAIN), beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
Functional Keywordslectin
Biological sourceLathyrus ochrus (yellow-flowered pea)
More
Total number of polymer chains4
Total formula weight53521.30
Authors
Bourne, Y.,Cambillau, C. (deposition date: 1993-01-27, release date: 1994-04-30, Last modification date: 2024-02-14)
Primary citationBourne, Y.,Rouge, P.,Cambillau, C.
X-ray structure of a biantennary octasaccharide-lectin complex refined at 2.3-A resolution.
J.Biol.Chem., 267:197-203, 1992
Cited by
PubMed Abstract: The structure and flexibility of saccharides have a profound and specific influence in several biological processes such as protein protection and the maintenance of conformational integrity, and in recognition events involving viruses, enzymes, and lectins. To establish the structural bases of these phenomena, we describe herein the extensively refined 2.3-A resolution x-ray structure of a biantennary octasaccharide of the N-acetyllactosamine type, complexed to isolectin I from Lathyrus ochrus. The two octasaccharides are located in clefts at each end of the long axis of the lectin. The conformations of both the lectin and the saccharide are slightly modified upon binding. The complex is stabilized by numerous hydrogen bonds, many of them involving water molecules. It is also stabilized by van der Waals interactions, including some with aromatic residues. A more general model of a possible lectin-glycoprotein interaction is also proposed.
PubMed: 1730588
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

227344

数据于2024-11-13公开中

PDB statisticsPDBj update infoContact PDBjnumon