1UGW

Crystal structure of jacalin- Gal complex

1UGW の概要

• エントリーDOI: 10.2210/pdb1ugw/pdb
• 関連するPDBエントリー: 1JAC 1M26 1UGX 1UGY 1UH0 1UH1
• 分子名称: Agglutinin alpha chain, Agglutinin beta-3 chain, Agglutinin alpha-chain, ... (5 entities in total)
• 機能のキーワード: all beta sheet protein, beta prism i fold, galactose specific, sugar binding protein
• 由来する生物種: Artocarpus integer; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 67543.26

構造登録者

Jeyaprakash, A.A.,Katiyar, S.,Swaminathan, C.P.,Sekar, K.,Surolia, A.,Vijayan, M. (登録日: 2003-06-22, 公開日: 2003-09-23, 最終更新日: 2023-10-25)

主引用文献

Jeyaprakash, A.A.,Katiyar, S.,Swaminathan, C.P.,Sekar, K.,Surolia, A.,Vijayan, M.
Structural Basis of the Carbohydrate Specificities of Jacalin: An X-ray and Modeling Study
J.MOL.BIOL., 332:217-228, 2003

PubMed Abstract: The structures of the complexes of tetrameric jacalin with Gal, Me-alpha-GalNAc, Me-alpha-T-antigen, GalNAcbeta1-3Gal-alpha-O-Me and Galalpha1-6Glc (mellibiose) show that the sugar-binding site of jacalin has three components: the primary site, secondary site A, and secondary site B. In these structures and in the two structures reported earlier, Gal or GalNAc occupy the primary site with the anomeric carbon pointing towards secondary site A. The alpha-substituents, when present, interact, primarily hydrophobically, with secondary site A which has variable geometry. O-H..., centered pi and C-H...pi hydrogen bonds involving this site also exist. On the other hand, beta-substitution leads to severe steric clashes. Therefore, in complexes involving beta-linked disaccharides, the reducing sugar binds at the primary site with the non-reducing end located at secondary site B. The interactions at secondary site B are primarily through water bridges. Thus, the nature of the linkage determines the mode of the association of the sugar with jacalin. The interactions observed in the crystal structures and modeling based on them provide a satisfactory qualitative explanation of the available thermodynamic data on jacalin-carbohydrate interactions. They also lead to fresh insights into the nature of the binding of glycoproteins by jacalin.

PubMed: 12946359
DOI: 10.1016/S0022-2836(03)00901-X

実験手法

X-RAY DIFFRACTION (1.7 Å)