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首页> 外文期刊>Journal of Molecular Biology >The N-terminal domain of Homer/Vesl is a new class II EVH1 domain.
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The N-terminal domain of Homer/Vesl is a new class II EVH1 domain.

机译：Homer / Vesl的N末端域是新的II类EVH1域。

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摘要

Cellular activities controlled by signal transduction processes such as cell motility and cell growth depend on the tightly regulated assembly of multiprotein complexes. Adapter proteins that specifically interact with their target proteins are key components required for the formation of these assemblies. Ena/VASP-homology 1 (EVH1) domains are small constituents of large modular proteins involved in microfilament assembly that specifically recognize proline-rich regions. EVH1 domain-containing proteins are present in neuronal cells, like the Homer/Vesl protein family that is involved in memory-generating processes. Here, we describe the crystal structure of the murine EVH1 domain of Vesl 2 at 2.2 A resolution. The small globular protein consists of a seven-stranded antiparallel beta-barrel with a C-terminal alpha-helix packing alongside the barrel. A shallow groove running parallel with beta-strand VI forms an extended peptide-binding site. Using peptide library screenings, we present data that demonstrate the high affinity of the Vesl 2 EVH1 domain towards peptide sequences containing a proline-rich core sequence (PPSPF) that requires additional charged amino acid residues on either side for specific binding. Our functional data, substantiated by structural data, demonstrate that the ligand-binding of the Vesl EVH1 domain differs from the interaction characteristics of the previously examined EVH1 domains of the Evl/Mena proteins. Analogous to the Src homology 3 (SH3) domains that bind their cognate ligands in two distinct directions, we therefore propose the existence of two distinct classes of EVH1 domains.
机译：受信号转导过程（例如细胞运动性和细胞生长）控制的细胞活动取决于严格调控的多蛋白复合物装配。与目标蛋白特异性相互作用的衔接蛋白是形成这些装配所需的关键组分。 Ena / VASP同源1（EVH1）域是微丝组装中涉及的大型模块化蛋白质的小成分，可特异性识别富含脯氨酸的区域。包含EVH1域的蛋白质存在于神经元细胞中，例如参与记忆生成过程的Homer / Vesl蛋白质家族。在这里，我们描述了Vesl 2的鼠EVH1域在2.2 A分辨率下的晶体结构。小球状蛋白由一个七链反平行β-桶和一个C-末端α-螺旋堆积在桶旁边组成。与β-链VI平行延伸的浅槽形成延伸的肽结合位点。使用肽库筛选，我们目前提供的数据表明，Vesl 2 EVH1结构域对含有富含脯氨酸核心序列（PPSPF）的肽序列具有高度亲和力，该序列需要在任一侧均需要额外的带电荷氨基酸残基才能进行特异性结合。由结构数据证实的我们的功能数据表明，Vesl EVH1结构域的配体结合不同于先前研究的Evl / Mena蛋白的EVH1结构域的相互作用特征。类似于在两个不同方向上结合其同源配体的Src同源3（SH3）域，我们因此建议存在两种不同类别的EVH1域。

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