3RS6

Crystal structure Dioclea virgata lectin in complexed with X-mannose

3RS6 の概要

• エントリーDOI: 10.2210/pdb3rs6/pdb
• 関連するPDBエントリー: 3RRD
• 分子名称: Lectin alpha chain, MANGANESE (II) ION, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: lectin, leguminose, carboydrate binding protein, x-mannose, seed dioclea virgata, sugar binding protein
• 由来する生物種: Dioclea virgata
• 細胞内の位置: Vacuole, aleurone grain: P58907
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25937.70

構造登録者

Gadelha, C.A.A.,Santi-Gadelha, T.,Nagano, C.S.,Bezerra, E.H.S.,Bezerra, M.J.B.,Alencar, K.L.,Silva-Filho, J.C. (登録日: 2011-05-02, 公開日: 2012-02-08, 最終更新日: 2024-02-28)

主引用文献

Batista da Nobrega, R.,Rocha, B.A.,Gadelha, C.A.,Santi-Gadelha, T.,Pires, A.F.,Assreuy, A.M.,Nascimento, K.S.,Nagano, C.S.,Sampaio, A.H.,Cavada, B.S.,Delatorre, P.
Structure of Dioclea virgata lectin: Relations between carbohydrate binding site and nitric oxide production.
Biochimie, 94:900-906, 2012

PubMed Abstract: The lectin of Dioclea virgata (DvirL), both native and complexed with X-man, was submitted to X-ray diffraction analysis and the crystal structure was compared to that of other Diocleinae lectins in order to better understand differences in biological properties, especially with regard to the ability of lectins to induce nitric oxide (NO) production. An association was observed between the volume of the carbohydrate recognition domain (CRD), the ability to induce NO production and the relative positions of Tyr12, Arg228 and Leu99. Thus, differences in biological activity induced by Diocleinae lectins are related to the configuration of amino acid residues in the carbohydrate binding site and to the structural conformation of subsequent regions capable of influencing site-ligand interactions. In conclusion, the ability of Diocleinae lectins to induce NO production depends on CRD configuration.

PubMed: 22198239
DOI: 10.1016/j.biochi.2011.12.009

実験手法

X-RAY DIFFRACTION (1.8 Å)