Graversen J H, Lorentsen R H, Jacobsen C, Moestrup S K, Sigurskjold B W, Thogersen H C, Etzerodt M
Laboratory of Gene Expression, Department of Molecular and Structural Biology, University of Aarhus, DK-8000 Aarhus C, Denmark.
J Biol Chem. 1998 Oct 30;273(44):29241-6. doi: 10.1074/jbc.273.44.29241.
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.
纤连蛋白是一种同三聚体蛋白，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，已知其能特异性结合纤溶酶原kringle 4蛋白结构域，这种相互作用对赖氨酸敏感。使用在大肠杆菌中产生的单残基和缺失突变体纤连蛋白衍生物进行的表面等离子体共振和等温滴定量热法结合分析表明，kringle 4结合位点位于碳水化合物识别结构域中，并且包括推定的碳水化合物结合位点的残基。此外，结合分析表明，除赖氨酸外，这种相互作用对钙也敏感。
