1n47

Isolectin B4 from Vicia villosa in complex with the Tn antigen

spinqualitylabelsall models 1n47, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1n47 is a 4 chain structure with sequence from Vicia villosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: A2G, CA, FUC, MN, NAG, SER Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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