四聚体
青刀豆
二聚体
化学
残留物(化学)
单体
结晶
刀豆蛋白A
四级结构
结晶学
生物化学
立体化学
有机化学
聚合物
酶
体外
基因
蛋白质亚单位
作者
Nam-Jin Chung,Yeo Reum Park,Dong-Heon Lee,Sun‐Young Oh,Jung Hee Park,Seung Jae Lee
出处
期刊:Journal of Microbiology and Biotechnology
[Springer Science+Business Media]
日期:2017-12-28
卷期号:27 (12): 2241-2244
被引量:5
标识
DOI:10.4014/jmb.1709.09057
摘要
The structure of concanavalin A (ConA) has been studied intensively owing to its specific interactions with carbohydrates and its heterometal (Ca²⁺ and Mn²⁺) coordination. Most structures from X-ray crystallography have shown ConA as a dimer or tetramer, because the complex formation requires specific crystallization conditions. Here, we reported the monomeric structure of ConA with a resolution of 1.6 Å, which revealed that metal coordination could trigger sugar-binding ability. The calcium coordination residue, Asn14, changed the orientation of carbohydrate-binding residues and biophysical details, including structural information, providing valuable clues for the development and application of detection kits using ConA.
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