1I3H

CONCANAVALIN A-DIMANNOSE STRUCTURE

1I3H の概要

• エントリーDOI: 10.2210/pdb1i3h/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900111
• 分子名称: Concanavalin-A, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose, MANGANESE (II) ION, ... (5 entities in total)
• 機能のキーワード: concanavalin a, protein-sugar complex, sugar binding protein
• 由来する生物種: Canavalia ensiformis (Jack bean); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26059.70

構造登録者

Sanders, D.A.R.,Moothoo, D.N.,Raftery, J.,Howard, A.J.,Helliwell, J.R.,Naismith, J.H. (登録日: 2001-02-15, 公開日: 2001-07-25, 最終更新日: 2024-02-07)

主引用文献

Sanders, D.A.,Moothoo, D.N.,Raftery, J.,Howard, A.J.,Helliwell, J.R.,Naismith, J.H.
The 1.2 A resolution structure of the Con A-dimannose complex.
J.Mol.Biol., 310:875-884, 2001

PubMed Abstract: The complex between concanavalin A (Con A) and alpha1-2 mannobiose (mannose alpha1-2 mannose) has been refined to 1.2 A resolution. This is the highest resolution structure reported for any sugar-lectin complex. As the native structure of Con A to 0.94 A resolution is already in the database, this gives us a unique opportunity to examine sugar-protein binding at high resolution. These data have allowed us to model a number of hydrogen atoms involved in the binding of the sugar to Con A, using the difference density map to place the hydrogen atoms. This map reveals the presence of the protonated form of Asp208 involved in binding. Asp208 is not protonated in the 0.94 A native structure. Our results clearly show that this residue is protonated and hydrogen bonds to the sugar. The structure accounts for the higher affinity of the alpha1-2 linked sugar when compared to other disaccharides. This structure identifies different interactions to those predicted by previous modelling studies. We believe that the additional data presented here will enable significant improvements to be made to the sugar-protein modelling algorithms.

PubMed: 11453694
DOI: 10.1006/jmbi.2001.4806

実験手法

X-RAY DIFFRACTION (1.2 Å)