Department of Biochemistry and Molecular Biology, Monash University, Clayton, Melbourne, VIC 3800, Australia.
Curr Opin Struct Biol. 2013 Dec;23(6):836-41. doi: 10.1016/j.sbi.2013.10.006. Epub 2013 Nov 16.
Plasminogen is the zymogen form of plasmin, an enzyme that plays a fundamental role in the dissolution of fibrin clots, the extracellular matrix and other key proteins involved in immunity and tissue repair. Comprising seven distinct domains (an N-terminal Pan-apple domain (PAp), 5 kringle domains (KR) and the serine protease domain (SP)), plasminogen undergoes a complex, incompletely understood conformational change that is key to its activation. Here, we review our current understanding of the structural basis for plasminogen activation with regard to new insights derived from crystallographic and biochemical studies.
纤溶酶原是纤溶酶的酶原形式，在溶解纤维蛋白凝块、细胞外基质和其他参与免疫和组织修复的关键蛋白方面发挥着基本作用。纤溶酶原由七个不同的结构域（一个 N 端泛苹果酸结构域（PAp）、5 个 kringle 结构域（KR）和丝氨酸蛋白酶结构域（SP））组成，经历一个复杂的、尚未完全理解的构象变化，这是其激活的关键。在这里，我们回顾了我们对纤溶酶原激活的结构基础的理解，以及从晶体学和生化研究中获得的新见解。
