Conformational differences in liganded and unliganded states of Galectin-3.
Conformational differences in liganded and unliganded states of Galectin-3.
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Galectin-3 配体和非配体状态的构象差异。
DOI：
10.1021/bi026671m
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发表时间：
2003
期刊：
影响因子：
--
通讯作者：
Prestegard,JH
中科院分区：
文献类型：
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作者：
Umemoto,Kimiko;Leffler,Hakon;Venot,Andre;Valafar,Homay;Prestegard,JH
Galectin-3（一种已知在哺乳动物系统中结合含有半乳糖的寡糖的凝集素）的碳水化合物识别结构域的构象已在不存在配体和存在 N-乙酰乳糖胺的情况下进行了研究。一种基于 NMR 谱中残留偶极耦合测量的新方法已被用来表征配体存在和不存在时沿主链的蛋白质结构差异，以及配体本身的结合几何形状。配体的数据与在络合状态的晶体结构中发现的配体结合几何形状一致。然而，在不存在配体的情况下，结合位点附近的主链环似乎发生了显着的重排。讨论了配体特异性和蛋白质功能的影响。
The conformation of the carbohydrate recognition domain of Galectin-3, a lectin known to bind galactose containing oligosaccharides in mammalian systems, has been investigated in the absence of ligand and in the presence ofN-acetylactosamine. A new methodology based on the measurement of residual dipolar couplings from NMR spectra has been used to characterize differences in protein structure along the backbone in the presence and absence of ligand, as well as the binding geometry of the ligand itself. The data on the ligand are consistent with the ligand binding geometry found in a crystal structure of the complexed state. However, a significant rearrangement of backbone loops near the binding site appears to occur in the absence of ligand. The implications for ligand specificity and protein functionality are discussed.