Purification, crystallization and preliminary characterization of an Eph-B2/ephrin-B2 complex
Purification, crystallization and preliminary characterization of an Eph-B2/ephrin-B2 complex
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DOI：
10.1107/s0907444902000264
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发表时间：
2002-03-01
期刊：
影响因子：
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通讯作者：
Nikolov, DB
中科院分区：
文献类型：
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作者：
Himanen, JP;Nikolov, DB
Eph受体及其肝配蛋白配体参与发育过程中细胞间通讯的各个方面，包括神经系统中轴突寻路过程和血管内皮细胞的细胞间相互作用。研究了EphB2受体的配体结合结构域和ephrin-B2的胞外结构域的识别和结合特性，并产生了它们的复合物的两种不同的共晶。一种晶型具有空间群C2，衍射至3.5埃，晶胞参数a = 128，B = 88，c = 79埃，β = 112度。另一种晶型在空间群P1中生长，晶胞参数a = 78，B = 78，c = 78埃，α = 69，β = 75，γ = 69度，衍射至2.7埃。使用后一种形式的结构测定实验正在进行中。该复合物的结构将阐明Eph受体和ephrin之间相互作用的化学性质，这将创造使用它们作为基于结构的抗癌药物开发靶点的可能性。
Eph receptors and their ephrin ligands are involved in various aspects of cell-cell communication during development, including those of the axon pathfinding processes in the nervous system and cell-cell interactions of the vascular endothelial cells. The recognition and binding properties of the ligand-binding domain of EphB2 receptor and the extracellular domain of ephrin-B2 have been studied and two different cocrystals of their complex have been generated. One crystal form has space group C2, diffracts to 3.5 Angstrom and has unit-cell parameters a = 128, b = 88, c = 79 Angstrom, beta = 112degrees. The other crystal form grows in space group P1, has unit-cell parameters a = 78, b = 78, c = 78 Angstrom, alpha = 69, beta = 75, gamma = 69degrees and diffracts to 2.7 Angstrom. Structure-determination experiments using the latter form are in progress. The structure of the complex will elucidate the chemical nature of the interactions between Eph receptors and ephrins, which would create the possibility of using them as targets for structure-based anticancer-drug development.