Crystal structure of tetranectin, a trimeric plasminogen‐binding protein with an α‐helical coiled coil

FEBS Letters

Larsen, Ingrid Kjøller¹  Etzerodt, Michael²  Rasmussen, Hanne¹  Kastrup, Jette Sandholm¹  Thøgersen, Hans Christian²  Nielsen, Bettina Bryde¹  Graversen, Jonas Heilskov²  Holtet, Thor Las² 

[1] Department of Medicinal Chemistry, Royal Danish School of Pharmacy, DK-2100 Copenhagen, Denmark;Laboratory of Gene Expression, Department of Molecular and Structural Biology, University of Aarhus, DK-8000 Aarhus C, Denmark

关键词: C-type lectin;    X-ray crystal structure;    Carbohydrate recognition domain;    Plasminogen;    Kringle 4;    α-Helical coiled coil;   

DOI  :  10.1016/S0014-5793(97)00664-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Tetranectin is a plasminogen kringle 4-binding protein. The crystal structure has been determined at 2.8 Å resolution using molecular replacement. Human tetranectin is a homotrimer forming a triple α-helical coiled coil. Each monomer consists of a carbohydrate recognition domain (CRD) connected to a long α-helix. Tetranectin has been classified in a distinct group of the C-type lectin superfamily but has structural similarity to the proteins in the group of collectins. Tetranectin has three intramolecular disulfide bridges. Two of these are conserved in the C-type lectin superfamily, whereas the third is present only in long-form CRDs. Tetranectin represents the first structure of a long-form CRD with intact calcium-binding sites. In tetranectin, the third disulfide bridge tethers the CRD to the long helix in the coiled coil. The trimerization of tetranectin as well as the fixation of the CRDs relative to the helices in the coiled coil indicate a demand for high specificity in the recognition and binding of ligands.

【 授权许可】

Unknown