1N47

Isolectin B4 from Vicia villosa in complex with the Tn antigen

Summary for 1N47

• Entry DOI: 10.2210/pdb1n47/pdb
• Descriptor: Isolectin B4, alpha-L-fucopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)]2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (7 entities in total)
• Functional Keywords: cancer antigen, vicia villosa lectin, glycoprotein tn-binding protein, carbohydrate recognition, sugar binding protein
• Biological source: Vicia villosa (hairy vetch)
• Total number of polymer chains: 4
• Total formula weight: 102808.82

Authors

Babino, A.,Tello, D.,Rojas, A.,Bay, S.,Osinaga, E.,Alzari, P.M. (deposition date: 2002-10-30, release date: 2003-02-25, Last modification date: 2024-10-30)

Primary citation

Babino, A.,Tello, D.,Rojas, A.,Bay, S.,Osinaga, E.,Alzari, P.M.
The crystal structure of a plant lectin in complex with the Tn antigen
FEBS Lett., 536:106-110, 2003

PubMed Abstract: The structure of the tetrameric Vicia villosa isolectin B4 (VVLB4) in complex with a cancer antigen, the Tn glycopeptide (GalNAc-O-Ser), was determined at 2.7 A resolution. The N-acetylgalactoside moiety of the ligand binds to the primary combining site of VVLB4 in a similar way as observed for other Gal/GalNAc-specific plant lectins. The amino acid moiety of the Tn antigen is largely exposed to the solvent and makes few contacts with the protein. The structure of the complex provides a framework to understand the differences in the strength of VVLB4 binding to different sugars and emphasizes the role of a single protein residue, Tyr127, as a structural determinant of Tn-binding specificity.

PubMed: 12586347
DOI: 10.1016/S0014-5793(03)00037-1

Experimental method

X-RAY DIFFRACTION (2.7 Å)