6TT9

rTBL Recombinant Lectin From Tepary Bean

これはPDB形式変換不可エントリーです。

6TT9 の概要

• エントリーDOI: 10.2210/pdb6tt9/pdb
• 分子名称: Phytohemagglutinin, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• 機能のキーワード: bean, cancer type glycans, tetrameric protein, leguminous lectin, b1-6 branched n-glycans, sugar binding protein
• 由来する生物種: Phaseolus acutifolius (Tepary bean)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 114158.65

構造登録者

Martinez Alarcon, D.,Varrot, A. (登録日: 2019-12-26, 公開日: 2020-05-13, 最終更新日: 2025-07-23)

主引用文献

Martinez-Alarcon, D.,Varrot, A.,Fitches, E.,Gatehouse, J.A.,Cao, M.,Pyati, P.,Blanco-Labra, A.,Garcia-Gasca, T.
Recombinant Lectin from Tepary Bean (Phaseolus acutifolius) with Specific Recognition for Cancer-Associated Glycans: Production, Structural Characterization, and Target Identification.
Biomolecules, 10:-, 2020

PubMed Abstract: Herein, we report the production of a recombinant Tepary bean lectin (TBL-1), its three-dimensional (3D) structure, and its differential recognition for cancer-type glycoconjugates. TBL-1 was expressed in yielding 316 mg per liter of culture, and was purified by nickel affinity chromatography. Characterization of the protein showed that TBL-1 is a stable 120 kDa homo-tetramer folded as a canonical leguminous lectin with two divalent cations (Ca and Mn) attached to each subunit, confirmed in its 3D structure solved by X-ray diffraction at 1.9 Å resolution. Monomers also presented a ~2.5 kDa -linked glycan located on the opposite face of the binding pocket. It does not participate in carbohydrate recognition but contributes to the stabilization of the interfaces between protomers. Screening for potential TBL-1 targets by glycan array identified 14 positive binders, all of which correspond to β1-6 branched -glycans' characteristics of cancer cells. The presence of α1-6 core fucose, also tumor-associated, improved carbohydrate recognition. TBL-1 affinity for a broad spectrum of mono- and disaccharides was evaluated by isothermal titration calorimetry (ITC); however, no interaction was detected, corroborating that carbohydrate recognition is highly specific and requires larger ligands for binding. This would explain the differential recognition between healthy and cancer cells by Tepary bean lectins.

PubMed: 32340396
DOI: 10.3390/biom10040654

実験手法

X-RAY DIFFRACTION (1.9 Å)