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首页> 外文期刊>Biochemistry >Solution structure and backbone dynamics of the functional cytoplasmic subdomain of human ephrin b2, a cell-surface ligand with bidirectional signaling properties.
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Solution structure and backbone dynamics of the functional cytoplasmic subdomain of human ephrin b2, a cell-surface ligand with bidirectional signaling properties.

机译：人ephrin b2（具有双向信号传递特性的细胞表面配体）的功能性细胞质亚域的溶液结构和骨干动力学。

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摘要

The cytoplasmic domain of B ephrins plays a central role in bidirectional signal transduction processes controlling pattern formation and morphogenesis, such as axon guidance, cell migration, segmentation, and angiogensis. In particular, the extremely conserved last 33-residue cytoplasmic subdomain was shown to bind to both a PDZ domain for one signaling pathway [Lu et al. (2001) Cell 105, 69-79] and an SH2 domain from an alternative signaling network [Cowan and Henkemeyer (2001) Nature 413, 174-179]. To date, no structural information is available for the cytoplasmic domain of ephrin B proteins. We report here a detailed NMR study on the structural and dynamic properties of the cytoplasmic domain of human ephrin B2. Our results reveal the following: (1) the N-terminal region of the cytoplasmic domain from residues 253 to 300 lacks the ability for structure formation and is particularly prone to aggregation; and (2) the C-terminal functional subdomain from residues 301 to 333 assumes two distinctive structural elements with residues 301-322 adopting a well-packed hairpin structure followed by a flexible C-terminal tail. Furthermore, the backbone (15)N relaxation data demonstrate that the hairpin structure has significantly limited backbone motions, indicating a high conformational stability for the folded structure. Therefore, while the flexible C-terminal tail is suitable for binding to the PDZ domain, the folded hairpin may represent a latent structure requiring phosphorylation-induced conformational changes for high-affinity interactions with the SH2 domain.
机译：B ephrins的胞质结构域在双向信号转导过程中起着核心作用，该过程控制着模式形成和形态发生，例如轴突引导，细胞迁移，分段和血管生成。特别地，显示极其保守的最后33个残基的胞质亚结构域结合一个信号途径的两个PDZ结构域[Lu等人，J.Biol.215：403-10]。 （2001）Cell 105，69-79]和来自替代信号网络的SH2域[Cowan and Henkemeyer（2001）Nature 413，174-179]。迄今为止，尚无关于ephrin B蛋白胞质结构域的结构信息。我们在这里报告了人类ephrin B2胞质域的结构和动态特性的详细NMR研究。我们的研究结果表明：（1）残基253至300的胞质结构域的N端区域缺乏结构形成能力，特别容易聚集。 （2）残基301至333的C末端功能子结构域假定两个独特的结构元件，其中残基301-322采用紧密包装的发夹结构，后接柔性C末端尾部。此外，骨架（15）N的松弛数据表明，发夹结构的骨架运动明显受限，表明折叠结构的构象稳定性高。因此，尽管柔性的C末端尾巴适合于结合PDZ结构域，但折叠的发夹可能代表潜在的结构，该结构需要磷酸化诱导的构象变化以实现与SH2结构域的高亲和力相互作用。

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