PseudoGTPase domains in p190RhoGAP proteins: a mini-review.
PseudoGTPase domains in p190RhoGAP proteins: a mini-review.
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p190RhoGAP 蛋白中的伪 GTP 酶结构域：小型综述。
DOI：
10.1042/bst20180481
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发表时间：
2018
影响因子：
3.9
通讯作者：
Boggon,TitusJ
中科院分区：
文献类型：
--
作者：
Stiegler,AmyL;Boggon,TitusJ
假酶通常缺乏可检测的催化活性，尽管采用了其催化活性对应物的整体蛋白质折叠，实际上“假”家族成员似乎被并入所有酶类别中。小GTP酶是重要的信号蛋白，最近的研究已经确定了许多新的家族成员与非典型残基的催化裂缝，称为pseudoGTP酶。为了说明该领域的最新发现，我们使用p190RhoGAP蛋白作为例子。p190RhoGAP蛋白（ARHGAP 5和ARHGAP 35）是Rho家族小GTP酶中最丰富的GTP酶激活蛋白。这些是Rho信号传导过程中的关键调节因子，如细胞迁移、粘附和胞质分裂。结构生物学补充和指导这些蛋白质的生化分析，并允许发现两个隐蔽的pseudoGTdR域，并重新分类的第三个，以前确定的，GTP酶折叠域作为一个pseudoGTdR。p190 RhoGAP蛋白内的三个结构域说明了这个快速扩展的假GTPase组的多样性。
Pseudoenzymes generally lack detectable catalytic activity despite adopting the overall protein fold of their catalytically competent counterparts, indeed ‘pseudo’ family members seem to be incorporated in all enzyme classes. The small GTPase enzymes are important signaling proteins, and recent studies have identified many new family members with noncanonical residues within the catalytic cleft, termed pseudoGTPases. To illustrate recent discoveries in the field, we use the p190RhoGAP proteins as an example. p190RhoGAP proteins (ARHGAP5andARHGAP35) are the most abundant GTPase activating proteins for the Rho family of small GTPases. These are key regulators of Rho signaling in processes such as cell migration, adhesion and cytokinesis. Structural biology has complemented and guided biochemical analyses for these proteins and has allowed discovery of two cryptic pseudoGTPase domains, and the re-classification of a third, previously identified, GTPase-fold domain as a pseudoGTPase. The three domains within p190RhoGAP proteins illustrate the diversity of this rapidly expanding pseudoGTPase group.