2D3S
Crystal Structure of basic winged bean lectin with Tn-antigen
Summary for 2D3S
| Entry DOI | 10.2210/pdb2d3s/pdb |
| Related | 1f9k 1fay 1wbf 1wbl |
| Descriptor | Basic agglutinin, alpha-L-fucopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)]2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-L-fucopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total) |
| Functional Keywords | legume lectin, glycosylated protein, agglutinin, tn-antigen, sugar binding protein |
| Biological source | Psophocarpus tetragonolobus (winged bean) |
| Total number of polymer chains | 4 |
| Total formula weight | 111835.87 |
| Authors | Kulkarni, K.A.,Sinha, S.,Katiyar, S.,Surolia, A.,Vijayan, M.,Suguna, K. (deposition date: 2005-10-01, release date: 2006-01-17, Last modification date: 2024-11-20) |
| Primary citation | Kulkarni, K.A.,Sinha, S.,Katiyar, S.,Surolia, A.,Vijayan, M.,Suguna, K. Structural basis for the specificity of basic winged bean lectin for the Tn-antigen: a crystallographic, thermodynamic and modelling study Febs Lett., 579:6775-6780, 2005 Cited by PubMed Abstract: The crystal structure of winged bean basic agglutinin in complex with GalNAc-alpha-O-Ser (Tn-antigen) has been elucidated at 2.35 angstroms resolution in order to characterize the mode of binding of Tn-antigen with the lectin. The Gal moiety occupies the primary binding site and makes interactions similar to those found in other Gal/GalNAc specific legume lectins. The nitrogen and oxygen atoms of the acetamido group of the sugar make two hydrogen bonds with the protein atoms whereas its methyl group is stabilized by hydrophobic interactions. A water bridge formed between the terminal oxygen atoms of the serine residue of the Tn-antigen and the side chain oxygen atom of Asn128 of the lectin increase the affinity of the lectin for Tn-antigen compared to that for GalNAc. A comparison with the available structures reveals that while the interactions of the glyconic part of the antigen are conserved, the mode of stabilization of the serine residue differs and depends on the nature of the protein residues in its vicinity. The structure provides a qualitative explanation for the thermodynamic parameters of the complexation of the lectin with Tn-antigen. Modeling studies indicate the possibility of an additional hydrogen bond with the lectin when the antigen is part of a glycoprotein. PubMed: 16310781DOI: 10.1016/j.febslet.2005.11.011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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