The crystal structure of a plant lectin in complex with the Tn antigen

FEBS Letters

Bay, Sylvie²  Tello, Diana³  Babino, Alvaro¹  Osinaga, Eduardo¹  Alzari, Pedro M³  Rojas, Adriana³ 

[1] Departamento de Bioquimica, Facultad de Medicina, Av. Gral Flores 2125, Montevideo, Uruguay;Unité de Chimie Organique (CNRS URA 2128), Institut Pasteur, 28 rue du Dr. Roux, 75724 Paris Cedex 15, France;Unité de Biochimie Structurale (CNRS URA 2185), Institut Pasteur, 25 rue du Dr. Roux, 75724 Paris Cedex 15, France

关键词: X-ray structure;    Cancer antigen;    Tn-binding protein;    Carbohydrate recognition;    Vicia villosa lectin;   

DOI  :  10.1016/S0014-5793(03)00037-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Å 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.

【 授权许可】

Unknown