1n47
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(New page: 200px<br /><applet load="1n47" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n47, resolution 2.70Å" /> '''Isolectin B4 from Vi...)
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Revision as of 19:49, 20 November 2007
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Isolectin B4 from Vicia villosa in complex with the Tn antigen
Overview
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.
About this Structure
1N47 is a Protein complex structure of sequences from Vicia villosa with CA, MN and TNR as ligands. Full crystallographic information is available from OCA.
Reference
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
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