The plasminogen binding site of the C-type lectin tetranectin is located in the carbohydrate recognition domain, and binding is sensitive to both calcium and lysine
The plasminogen binding site of the C-type lectin tetranectin is located in the carbohydrate recognition domain, and binding is sensitive to both calcium and lysine
复制标题
DOI：
10.1074/jbc.273.44.29241
复制
发表时间：
1998-10-30
影响因子：
4.8
通讯作者：
Etzerodt, M
中科院分区：
文献类型：
--
作者：
Graversen, JH;Lorentsen, RH;Etzerodt, M
四连接素是一种同源三聚体蛋白，属于C型凝集素家族，在结构上与甘露糖结合蛋白的相应区域高度相关，已知其特异性结合纤溶酶原kringle 4蛋白结构域，这是一种对赖氨酸敏感的相互作用。表面等离子体共振和等温量热法结合分析，使用单残基和缺失突变体的四连接素衍生物在大肠杆菌中产生的结果表明，Kringle 4结合位点驻留在碳水化合物识别域，包括残基的推定的碳水化合物结合位点。此外，结合分析表明，除了赖氨酸的相互作用是敏感的钙。
Tetranectin, a homotrimeric protein belonging to the family of C-type lectins and structurally highly related to corresponding regions of the mannose-binding proteins, is known specifically to bind the plasminogen kringle 4 protein domain, an interaction sensitive to lysine. Surface plasmon resonance and isothermal calorimetry binding analyses using single-residue and deletion mutant tetranectin derivatives produced in Escherichia coli showed that the kringle 4 binding site resides in the carbohydrate recognition domain and includes residues of the putative carbohydrate binding site. Furthermore, the binding analysis revealed that the interaction is sensitive to calcium in addition to lysine.