Phospholipase D (PLD) and its metabolic active product phosphatidic acid (PA) engage in a wide range of physiopathologic processes in the cell. PLDs have been considered as a potential and promising drug target. Recently, the crystal structures of PLDs in mammalian and plant have been solved at atomic resolution. These achievements allow us to understand the structural differences among different species of PLDs and the functions of their key domains. In this review, we summarize the sequence and structure of different species of PLD isoforms, and discuss the structural mechanisms for PLD interactions with their binding partners and the functions of each key domain in the regulation of PLDs activation and catalytic reaction.

磷脂酶 D (PLD) 及其代谢活性产物磷脂酸 (PA) 在细胞中参与广泛的病理生理过程。PLDs被认为是一种潜在的和有前途的药物靶点。最近，哺乳动物和植物中PLD的晶体结构已经在原子分辨率下得到解决。这些成就使我们能够了解不同PLD种类之间的结构差异及其关键域的功能。在这篇综述中，我们总结了不同种类的PLD亚型的序列和结构，并讨论了PLD与其结合伙伴相互作用的结构机制以及每个关键域在调节PLDs活化和催化反应中的作用。