Domain swapping within PDZ2 is responsible for dimerization of ZO proteins
Domain swapping within PDZ2 is responsible for dimerization of ZO proteins
复制标题
DOI：
10.1074/jbc.m707255200
复制
发表时间：
2007-12-28
影响因子：
4.8
通讯作者：
Lavie, Arnon
中科院分区：
文献类型：
--
作者：
Fanning, Alan S.;Lye, Ming F.;Lavie, Arnon
ZO-1 是一种参与细胞-细胞连接的多结构域蛋白，包含三个 PDZ 结构域，这是其体内功能所必需的。 PDZ 结构域通过识别其他蛋白质上的短肽基序的能力，在组装不同的蛋白质复合物中发挥着核心作用。我们确定了 ZO-1 三个 PDZ 结构域中的第二个结构域，已知该结构域可促进二聚化并与连接蛋白上的 C 端序列结合。二聚体通过β链的广泛对称结构域交换来稳定，这与任何其他已知的PDZ二聚机制不同。典型的肽结合沟在 PDZ2 二聚体的两个亚基中保持完整，并且由两个单体贡献的元件创建。这种独特的结构揭示了 PDZ 结构域如何二聚化的另一个例子，并对体内肽结合和寡聚化具有多重影响。
ZO-1 is a multidomain protein involved in cell- cell junctions and contains three PDZ domains, which are necessary for its function in vivo. PDZ domains play a central role in assembling diverse protein complexes through their ability to recognize short peptide motifs on other proteins. We determined the structure of the second of the three PDZ domains of ZO-1, which is known to promote dimerization as well as bind to C-terminal sequences on connexins. The dimer is stabilized by extensive symmetrical domain swapping of beta-strands, which is unlike any other known mechanism of PDZ dimerization. The canonical peptide-binding groove remains intact in both subunits of the PDZ2 dimer and is created by elements contributed from both monomers. This unique structure reveals an additional example of how PDZ domains dimerize and has multiple implications for both peptide binding and oligomerization in vivo.