Anashkin V A, Baykov A A, Lahti R
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119992, Russia.
Biochemistry (Mosc). 2017 Oct;82(10):1079-1087. doi: 10.1134/S0006297917100017.
Cystathionine β-synthase (CBS) domains discovered 20 years ago can bind different adenosine derivatives (AMP, ADP, ATP, S-adenosylmethionine, NAD, diadenosine polyphosphates) and thus regulate the activities of numerous proteins. Mutations in CBS domains of enzymes and membrane transporters are associated with several hereditary diseases. The regulatory unit is a quartet of CBS domains that belong to one or two polypeptides and usually form a conserved disk-like structure. CBS domains function as "internal inhibitors" in enzymes, and their bound ligands either amplify or attenuate the inhibitory effect. Recent studies have opened a way to understanding the structural basis of enzyme regulation via CBS domains and widened the list of their bound ligands.
20年前发现的胱硫醚β-合酶（CBS）结构域能够结合不同的腺苷衍生物（AMP、ADP、ATP、S-腺苷甲硫氨酸、NAD、二腺苷多磷酸），从而调节众多蛋白质的活性。酶和膜转运蛋白的CBS结构域中的突变与多种遗传性疾病相关。调节单元是由属于一条或两条多肽的四个CBS结构域组成的四重体，通常形成一个保守的盘状结构。CBS结构域在酶中起“内部抑制剂”的作用，其结合的配体要么增强要么减弱抑制作用。最近的研究为理解通过CBS结构域进行酶调节的结构基础开辟了道路，并扩大了其结合配体的种类。
