Ponting C P, Marshall J M, Cederholm-Williams S A
Department of Biochemistry, University of Oxford, UK.
Blood Coagul Fibrinolysis. 1992 Oct;3(5):605-14.
Plasminogen is the zymogen form of plasmin, a broad specificity serine protease whose activity contributes to a variety of normal and pathological conditions, including intravascular thrombolysis and extracellular proteolysis. Plasminogen contains seven structural units or 'domains', each of which confer specific properties on the molecule. The kringle domains possess fibrin-binding functions and, together with the N-terminal peptide, regulate the ability of plasminogen to adopt at least three dissimilar conformations. These conformational forms influence the rate of formation, following activation by plasminogen activators, of the plasmin active site within its C-terminal serine protease domain. Structural and functional analogies are postulated between these plasminogen structures and the conformations of other proteins related by sequence homology.
纤溶酶原是纤溶酶的酶原形式，纤溶酶是一种具有广泛特异性的丝氨酸蛋白酶，其活性参与多种正常和病理生理过程，包括血管内溶栓和细胞外蛋白水解。纤溶酶原包含七个结构单元或“结构域”，每个结构域赋予分子特定的性质。kringle结构域具有纤维蛋白结合功能，并与N端肽一起调节纤溶酶原采取至少三种不同构象的能力。这些构象形式影响纤溶酶原激活剂激活后，其C端丝氨酸蛋白酶结构域内纤溶酶活性位点的形成速率。推测这些纤溶酶原结构与通过序列同源性相关的其他蛋白质的构象之间存在结构和功能上的相似性。
