Structural highlights
Function
[LEC_VICVI] N-acetyl-D-galactosamine specific lectin. Binds the Tn determinant (GalNAc-alpha-O-Ser/Thr) of the tumor-associated glycopeptide. Could be required for agglutinating cells such as Tn-exposed erythrocytes.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
The crystal structure of a plant lectin in complex with the Tn antigen.,Babino A, Tello D, Rojas A, Bay S, Osinaga E, Alzari PM FEBS Lett. 2003 Feb 11;536(1-3):106-10. PMID:12586347[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Babino A, Tello D, Rojas A, Bay S, Osinaga E, Alzari PM. The crystal structure of a plant lectin in complex with the Tn antigen. FEBS Lett. 2003 Feb 11;536(1-3):106-10. PMID:12586347
