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Journal articles
The crystal structure of a plant lectin in complex with the Tn antigen.
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.
https://hal-pasteur.archives-ouvertes.fr/pasteur-00166854
Contributor : Sylvie Bay Connect in order to contact the contributor
Submitted on : Friday, August 10, 2007 - 3:08:07 PM
Last modification on : Tuesday, October 19, 2021 - 10:25:51 PM
Contributor : Sylvie Bay Connect in order to contact the contributor
Submitted on : Friday, August 10, 2007 - 3:08:07 PM
Last modification on : Tuesday, October 19, 2021 - 10:25:51 PM
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