4U36
Crystal structure of a seed lectin from Vatairea macrocarpa complexed with Tn-antigen
4U36 の概要
エントリーDOI | 10.2210/pdb4u36/pdb |
関連するPDBエントリー | 4U2A |
分子名称 | Seed lectin, MANGANESE (II) ION, CALCIUM ION, ... (8 entities in total) |
機能のキーワード | lectin, legume, dalbergieae, tn-antigen, sugar binding protein |
由来する生物種 | Vatairea macrocarpa |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 27219.65 |
構造登録者 | Sousa, B.L.,Silva-Filho, J.C.,Kumar, P.,Lyskowski, A.,Bezerra, G.A.,Delatorre, P.,Rocha, B.A.M.,Nagano, C.S.,Gruber, K.,Cavada, B.S. (登録日: 2014-07-18, 公開日: 2014-12-31, 最終更新日: 2023-09-27) |
主引用文献 | Sousa, B.L.,Silva Filho, J.C.,Kumar, P.,Pereira, R.I.,yskowski, A.,Rocha, B.A.,Delatorre, P.,Bezerra, G.A.,Nagano, C.S.,Gruber, K.,Cavada, B.S. High-resolution structure of a new Tn antigen-binding lectin from Vatairea macrocarpa and a comparative analysis of Tn-binding legume lectins. Int.J.Biochem.Cell Biol., 59C:103-110, 2014 Cited by PubMed Abstract: Plant lectins have been studied as histological markers and promising antineoplastic molecules for a long time, and structural characterization of different lectins bound to specific cancer epitopes has been carried out successfully. The crystal structures of Vatairea macrocarpa (VML) seed lectin in complex with GalNAc-α-O-Ser (Tn antigen) and GalNAc have been determined at the resolution of 1.4Å and 1.7Å, respectively. Molecular docking analysis of this new structure and other Tn-binding legume lectins to O-mucin fragments differently decorated with this antigen provides a comparative binding profile among these proteins, stressing that subtle alterations that may not influence monosaccharide binding can, nonetheless, directly impact the ability of these lectins to recognize naturally occurring antigens. In addition to the specific biological effects of VML, the structural and binding similarities between it and other lectins commonly used as histological markers (e.g., VVLB4 and SBA) strongly suggest VML as a candidate tool for cancer research. PubMed: 25499445DOI: 10.1016/j.biocel.2014.12.002 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.4 Å) |
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