5JM1

Structure of tetrameric jacalin complexed with a trisaccharide, Gal alpha-(1,3) Gal beta-(1,4) Gal

5JM1 の概要

• エントリーDOI: 10.2210/pdb5jm1/pdb
• 分子名称: Agglutinin alpha chain, Agglutinin beta-3 chain, alpha-D-galactopyranose-(1-3)-beta-D-galactopyranose-(1-4)-beta-D-galactopyranose, ... (7 entities in total)
• 機能のキーワード: plant lectins, sugar binding protein, galactose specific lectin, beta-prism i fold, post translational proteolysis, t-antigen binding protein, reducing, non-reducing sugars
• 由来する生物種: Artocarpus integer (Jack fruit); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 67896.02

構造登録者

Abhinav, K.V.,Sharma, K.,Surolia, A.,Vijayan, M. (登録日: 2016-04-28, 公開日: 2016-12-14, 最終更新日: 2023-11-08)

主引用文献

Abhinav, K.V.,Sharma, K.,Surolia, A.,Vijayan, M.
Effect of linkage on the location of reducing and nonreducing sugars bound to jacalin.
IUBMB Life, 68:971-979, 2016

PubMed Abstract: The crystal structures of jacalin complexed with Gal α-(1,4) Gal and Gal α-(1,3) Gal β-(1,4) Gal have been determined with the primary objective of exploring the effect of linkage on the location of reducing and non-reducing sugars in the extended binding site of the lectin, an issue which has not been studied thoroughly. Contrary to the earlier surmise based on simple steric considerations, the two structures demonstrate that α-linked sugars can bind to jacalin with nonreducing sugar at the primary binding site. This is made possible substantially on account of the hitherto underestimated plasticity of a non-polar region of the extended binding site. Modeling studies involving conformational search and energy minimization, along with available crystallographic and thermodynamic data, indicate a strong preference for complexation with Gal β-(1,3) Gal with the reducing Gal at the primary site, followed by that with Gal α-(1,3) Gal, with the reducing or non-reducing Gal located at the primary binding site. This observation is in consonance with the facility of jacalin to bind mucin type O-glycans containing T-antigen core. © 2016 IUBMB Life, 68(12):971-979, 2016.

PubMed: 27808459
DOI: 10.1002/iub.1572

実験手法

X-RAY DIFFRACTION (1.95 Å)