Thornberry N A, Molineaux S M
Department of Enzymology, Merck Research Laboratories, Rahway, New Jersey 07065, USA.
Protein Sci. 1995 Jan;4(1):3-12. doi: 10.1002/pro.5560040102.
Interleukin-1 beta converting enzyme is the first member of a new class of cysteine proteases. The most distinguishing feature of this family is a nearly absolute specificity for cleavage at aspartic acid. This enzyme has been the subject of intense research because of its role in the production of IL-1 beta, a key mediator of inflammation. These studies have culminated in the design of potent inhibitors and determination of its crystal structure. The structure secures the relationship of the enzyme to CED-3, the product of a gene required for programmed cell death in Caenorhabditis elegans, suggesting that members of this family function in cell death in vertebrates.
白细胞介素-1β转化酶是一类新型半胱氨酸蛋白酶的首个成员。该家族最显著的特征是对天冬氨酸处的切割具有近乎绝对的特异性。由于其在白细胞介素-1β(炎症的关键介质)产生过程中的作用,这种酶一直是深入研究的对象。这些研究最终促成了强效抑制剂的设计并确定了其晶体结构。该结构确定了这种酶与CED-3(秀丽隐杆线虫程序性细胞死亡所需基因的产物)之间的关系,这表明该家族成员在脊椎动物的细胞死亡中发挥作用。