2000/03/27 by Rikke Høegh Lorentsen, Rikke H. LORENTSEN, Jonas H. GRAVERSEN +6
Biochemistry, Genetics and Molecular Biology · Medicine · #Cell Adhesion Molecules Research #Protease and Inhibitor Mechanisms #Signaling Pathways in Disease
paper · doi:10.1042/bj3470083
openalex publication_date 2000/03/27 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/29
Tetranectin is a homotrimeric plasma and extracellular-matrix protein that binds plasminogen and complex sulphated polysaccharides including heparin. In terms of primary and tertiary structure, tetranectin is related to the collectin family of Ca(2+)-binding C-type lectins. Tetranectin is encoded in three exons. Exon 3 encodes the carbohydrate recognition domain, which binds to kringle 4 in plasminogen at low levels of Ca(2+). Exon 2 encodes an alpha-helix, which is necessary and sufficient to govern the trimerization of tetranectin by assembling into a triple-helical coiled-coil structural element. Here we show that the heparin-binding site in tetranectin resides not in the carbohydrate recognition domain but within the N-terminal region, comprising the 16 amino acid residues encoded by exon 1. In particular, the lysine residues in the decapeptide segment KPKKIVNAKK (tetranectin residues 6-15) are shown to be of primary importance in heparin binding.