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1LTE

STRUCTURE OF A LEGUME LECTIN WITH AN ORDERED N-LINKED CARBOHYDRATE IN COMPLEX WITH LACTOSE

Summary for 1LTE
Entry DOI10.2210/pdb1lte/pdb
Related PRD IDPRD_900004
DescriptorCORAL TREE LECTIN, Xylitol-(1-2)-[alpha-D-mannopyranose-(1-3)][alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, ... (6 entities in total)
Functional Keywordslectin
Biological sourceErythrina corallodendron (coral tree)
Total number of polymer chains1
Total formula weight27879.61
Authors
Shaanan, B.,Lis, H.,Sharon, N. (deposition date: 1991-06-25, release date: 1994-01-31, Last modification date: 2024-11-06)
Primary citationShaanan, B.,Lis, H.,Sharon, N.
Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose.
Science, 254:862-866, 1991
Cited by
PubMed Abstract: The three-dimensional structure of the lactose complex of the Erythrina corallodendron lectin (EcorL), a dimer of N-glycosylated subunits, was determined crystallographically and refined at 2.0 angstrom resolution to an R value of 0.19. The tertiary structure of the subunit is similar to that of other legume lectins, but interference by the bulky N-linked heptasaccharide, which is exceptionally well ordered in the crystal, forces the EcorL dimer into a drastically different quaternary structure. Only the galactose moiety of the lactose ligand resides within the combining site. The galactose moiety is oriented differently from ligands in the mannose-glucose specific legume lectins and is held by hydrophobic interactions with Ala88, Tyr106, Phe131, and Ala218 and by seven hydrogen bonds, four of which are to the conserved Asp89, Asn133, and NH of Gly107. The specificity of legume lectins toward the different C-4 epimers appears to be associated with extensive variations in the outline of the variable parts of the binding sites.
PubMed: 1948067
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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