Isolated ZP-N domains constitute the n-terminal extensions of zona pellucida proteins
Isolated ZP-N domains constitute the n-terminal extensions of zona pellucida proteins
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DOI：
10.1093/bioinformatics/btm265
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发表时间：
2007-08-01
期刊：
影响因子：
5.8
通讯作者：
Monget, Philippe
中科院分区：
文献类型：
--
作者：
Callebaut, Isabelle;Mornon, Jean-Paul;Monget, Philippe
透明带（Zona Pellucida，ZP）结构域广泛存在于多种细胞外蛋白中，在细胞外蛋白的聚合过程中起重要作用。它们由ZP蛋白共享，ZP蛋白构成动物卵的细胞外被。除了ZP 3，构成初级精子受体，ZP蛋白具有，除了它们的C-末端ZP结构域，N-末端延伸，这被认为是在物种特异性配子识别中发挥重要作用。在这里，我们表明，这些扩展是由单个或多个拷贝的一个小的球状域，这可以显着相关的N-末端区域的ZP域（ZP-N域）。这一发现为ZP蛋白的分子进化带来了新的见解，ZP蛋白可能围绕一个共同的ZP-N结构进化，并且更普遍地进入ZP-N结构域的明显序列多样性，ZP-N结构域可以作为分离的亚基或与ZP-C结构域紧密相关以形成完整的典型ZP结构域。
Zona Pellucida (ZP) domains have been found in a wide variety of extracellular proteins, in which they play essential role for polymerization. They are shared by the ZP proteins, which constitute the extracellular coat of animal eggs. Except from ZP3, constituting the primary sperm receptor, the ZP proteins possess, in addition to their C-terminal ZP domains, N-terminal extensions, which are thought to play an important role in the species-specific gamete recognition. Here, we show that these extensions are made of single or multiple copies of a small globular domain, which can be significantly related to the N-terminal region of ZP domains (ZP-N domains). This finding brings new insights into the molecular evolution of ZP proteins, which may have evolved around a common ZP-N architecture, and more generally into the noticeable sequence diversity of ZP-N domains, which can be found as isolated subunits or tightly associated with ZP-C domains to form complete, canonical ZP domains.