Crystal structure of streptokinase beta-domain.
Crystal structure of streptokinase beta-domain.
复制标题
链激酶β结构域的晶体结构。
DOI：
10.1016/s0014-5793(99)01214-4
复制
发表时间：
1999
期刊：
影响因子：
3.5
通讯作者：
Zhang,XC
中科院分区：
文献类型：
--
作者：
Wang,X;Tang,J;Hunter,B;Zhang,XC
链激酶（Streptokinase）是溶血性链球菌的一种47 kDa分泌蛋白，是一种人类纤溶酶原激活剂，包含三个由柔性环连接的结构域。我们在这里描述了在2.4 Å分辨率下分离的链激酶中间（SKβ）结构域的晶体结构。在功能上重要的结构特征中，纤溶酶原kringle结构域的推定结合位点位于完全暴露的发夹环的尖端。SKβ基因保守残基的分布与其功能密切相关。SKβ二聚体的广泛界面表明，这种二聚体也可能存在于游离SKβ的溶液中。
Streptokinase, a 47 kDa secreted protein of hemolytic strains of streptococci, is a human plasminogen activator and contains three structural domains linked by flexible loops. We describe here the crystal structure of the isolated streptokinase middle (SKβ) domain determined at 2.4 Å resolution. Among the functionally important structural features is a putative binding site for a kringle domain of plasminogen located at the tip of a fully exposed hairpin loop. The distribution of genetically conserved residues of SKβ is strongly correlated with their functions. The extensive interface of the SKβ dimer suggests that such dimers may also exist in solution for free SKβ.