High-resolution crystal structures of Erythrina cristagalli lectin in complex with lactose and 2′-α-L-fucosyllactose and correlation with thermodynamic binding data
High-resolution crystal structures of Erythrina cristagalli lectin in complex with lactose and 2′-α-L-fucosyllactose and correlation with thermodynamic binding data
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DOI：
10.1016/s0022-2836(02)00554-5
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发表时间：
2002-08-02
影响因子：
5.6
通讯作者：
Krengel, U
中科院分区：
文献类型：
--
作者：
Svensson, C;Teneberg, S;Krengel, U
用质谱法对鸡冠花凝集素（Erythrinacristagalli lectin，ECL）的一级序列进行了分析，并分别在1.6埃和1.7埃分辨率下测定了该凝集素与乳糖和2 '-α-L-岩藻糖基乳糖复合物的晶体结构。将这两种复合物与密切相关的刺桐凝集素（ECorL）与乳糖复合物的晶体结构、荆豆凝集素II与2 ′-α-L-岩藻糖基乳糖复合物的晶体结构以及ECorL与2 ′-α-L-岩藻糖基-N-乙酰基乳糖胺的两种模拟复合物进行了比较。分子模型与ECL与2 '-U复合物的晶体结构非常相似。L-岩藻糖基乳糖相对于结合的整体模式，L-岩藻糖紧密地配合到由Tyr 106，TyrI 08，Trp 135和Pro 134包围的空腔中，邻接。凝集素的主要结合位点。然而，在氢键和疏水相互作用的网络中的L-岩藻糖的凝集素的结合位点，指出模型和实验结构之间的显着差异，指出建模方法的局限性。除了ECL复合物的结构表征，努力进行相关的结构数据与从微量热法获得的热力学数据，揭示了水网络中的凝集素结合位点的碳水化合物结合的重要性。(C)2002爱思唯尔科技有限公司。保留所有权利。
The primary sequence of Erythrina cristagalli lectin (ECL) was mapped by mass spectrometry, and the crystal structures of the lectin in complex with lactose and 2'-alpha-L-fucosyllactose were determined at 1.6 Angstrom and 1.7 Angstrom resolution, respectively. The two complexes were compared with the crystal structure of the closely related Erythrina corallodendron lectin (ECorL) in complex with lactose, with the crystal structure of the Ulex europaeus lectin II in complex with 2'-alpha-L-fucosyllactose, and with two modeled complexes of ECorL with 2'-alpha-L-fucosyl-N-acetyllactosamine. The molecular models are very similar to the crystal structure of ECL in complex with 2'-U.-L-fucosyllactose with respect to the overall mode of binding, with the L-fucose fitting snugly into the cavity surrounded by Tyr106, TyrI08, Trp135 and Pro134 adjoining the. primary combining site of the lectin. Marked differences were however noted between the models and the experimental structure in the network of hydrogen bonds and hydrophobic interactions holding the L-fucose in the combining site of the lectin, pointing to limitations of the modeling approach. In addition to the structural characterization of the ECL complexes, an effort was undertaken to correlate the structural data with thermodynamic data obtained from microcalorimetry, revealing the importance of the water network in the lectin combining site for carbohydrate binding. (C) 2002 Elsevier Science Ltd. All rights reserved.