4R6P

Jacalin-carbohydrate interactions. Distortion of the ligand as a determinant of affinity.

4R6P の概要

• エントリーDOI: 10.2210/pdb4r6p/pdb
• 関連するPDBエントリー: 1JAC 1KU8 1M26 1UGW 1UGY 1UH0 4R6N 4R6O 4R6Q 4R6R
• 分子名称: Agglutinin alpha chain, Agglutinin beta-3 chain, ISOPROPYL ALCOHOL, ... (7 entities in total)
• 機能のキーワード: galactose specific lectin, beta-prism i fold, post translational proteolysis, t-antigen binding protein, plant lectins, galactose, sugar binding protein
• 由来する生物種: Artocarpus integer (campedak,chempedak); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 67113.37

構造登録者

Abhinav, K.V.,Sharma, K.,Swaminathan, C.P.,Surolia, A.,Vijayan, M. (登録日: 2014-08-26, 公開日: 2015-02-18, 最終更新日: 2023-11-08)

主引用文献

Abhinav, K.V.,Sharma, K.,Swaminathan, C.P.,Surolia, A.,Vijayan, M.
Jacalin-carbohydrate interactions: distortion of the ligand molecule as a determinant of affinity.
Acta Crystallogr.,Sect.D, 71:324-331, 2015

PubMed Abstract: Jacalin is among the most thoroughly studied lectins. Its carbohydrate-binding site has also been well characterized. It has been postulated that the lower affinity of β-galactosides for jacalin compared with α-galactosides is caused by steric interactions of the substituents in the former with the protein. This issue has been explored energetically and structurally using different appropriate carbohydrate complexes of jacalin. It turns out that the earlier postulation is not correct. The interactions of the substituent with the binding site remain essentially the same irrespective of the anomeric nature of the substitution. This is achieved through a distortion of the sugar ring in β-galactosides. The difference in energy, and therefore in affinity, is caused by a distortion of the sugar ring in β-galactosides. The elucidation of this unprecedented distortion of the ligand as a strategy for modulating affinity is of general interest. The crystal structures also provide a rationale for the relative affinities of the different carbohydrate ligands for jacalin.

PubMed: 25664742
DOI: 10.1107/S139900471402553X

実験手法

X-RAY DIFFRACTION (1.7 Å)