The PB1 domain and the PC motif-containing region are structurally similar protein binding modules
The PB1 domain and the PC motif-containing region are structurally similar protein binding modules
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DOI：
10.1093/emboj/cdg475
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发表时间：
2003-10-01
期刊：
影响因子：
11.4
通讯作者：
Inagaki, F
中科院分区：
文献类型：
--
作者：
Yoshinaga, S;Kohjima, M;Inagaki, F
PC基序与PB 1结构域（含PC基序蛋白的结合伴侣）一起在进化上是保守的。为了与PB 1结构域相互作用，需要包含PC基序及其侧翼区的含有PC基序的区域（PCCR）。由于PB 1结构域和PCCR是在多种信号蛋白中发现的新型结合模块，因此它们的结构和功能表征至关重要。Bem 1 p和Cdc 24 p通过PB 1-PCCR相互作用调节芽殖酵母细胞的极化。在这里，我们通过NMR确定了Cdc 24 p的PCCR的三级结构。PCCR的三级结构类似于Bem 1 p的PB 1结构域，其被分类为泛素折叠。PC基序部分采取紧凑的β-β-α-折叠，呈现在泛素支架上。突变研究表明，PB 1-PCCR的相互作用主要是静电。基于结构信息，我们将PB 1结构域和PCCR组合成一个新的家族，命名为PB 1家族。因此，PB 1家族蛋白彼此形成特异性二聚体。
The PC motif is evolutionarily conserved together with the PB1 domain, a binding partner of the PC motif-containing protein. For interaction with the PB1 domain, the PC motif-containing region (PCCR) comprising the PC motif and its flanking regions is required. Because the PB1 domain and the PCCR are novel binding modules found in a variety of signaling proteins, their structural and functional characterization is crucial. Bem1p and Cdc24p interact through the PB1-PCCR interaction and regulate cell polarization in budding yeast. Here, we determined a tertiary structure of the PCCR of Cdc24p by NMR. The tertiary structure of the PCCR is similar to that of the PB1 domain of Bem1p, which is classified into a ubiquitin fold. The PC motif portion takes a compact betabetaalpha-fold, presented on the ubiquitin scaffold. Mutational studies indicate that the PB1-PCCR interaction is mainly electrostatic. Based on the structural information, we group the PB1 domains and the PCCRs into a novel family, named the PB1 family. Thus, the PB1 family proteins form a specific dimer with each other.