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4D69

SOYBEAN AGGLUTININ FROM GLYCINE MAX IN COMPLEX WITH THE ANTIGEN Tn

Summary for 4D69
Entry DOI10.2210/pdb4d69/pdb
DescriptorLECTIN, SHORT ANTIGEN PEPTIDE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
Functional Keywordssugar-binding protein, sugar binding protein
Biological sourceGLYCINE MAX (SOYBEAN)
More
Total number of polymer chains24
Total formula weight346930.73
Authors
Primary citationMadariaga, D.,Martinez-Saez, N.,Somovilla, V.J.,Coelho, H.,Valero-Gonzalez, J.,Castro-Lopez, J.,Asensio, J.L.,Jimenez-Barbero, J.,Busto, J.H.,Avenoza, A.,Marcelo, F.,Hurtado-Guerrero, R.,Corzana, F.,Peregrina, J.M.
Detection of Tumor-Associated Glycopeptides by Lectins: The Peptide Context Modulates Carbohydrate Recognition.
Acs Chem.Biol., 10:747-, 2015
Cited by
PubMed Abstract: Tn antigen (α-O-GalNAc-Ser/Thr) is a convenient cancer biomarker that is recognized by antibodies and lectins. This work yields remarkable results for two plant lectins in terms of epitope recognition and reveals that these receptors show higher affinity for Tn antigen when it is incorporated in the Pro-Asp-Thr-Arg (PDTR) peptide region of mucin MUC1. In contrast, a significant affinity loss is observed when Tn antigen is located in the Ala-His-Gly-Val-Thr-Ser-Ala (AHGVTSA) or Ala-Pro-Gly-Ser-Thr-Ala-Pro (APGSTAP) fragments. Our data indicate that the charged residues, Arg and Asp, present in the PDTR sequence establish noteworthy fundamental interactions with the lectin surface as well as fix the conformation of the peptide backbone, favoring the presentation of the sugar moiety toward the lectin. These results may help to better understand glycopeptide-lectin interactions and may contribute to engineer new binding sites, allowing novel glycosensors for Tn antigen detection to be designed.
PubMed: 25457745
DOI: 10.1021/CB500855X
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

238268

数据于2025-07-02公开中

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