The heparin-binding site in tetranectin is located in the N-terminal region and binding does not involve the carbohydrate recognition domain
| Autor: | Lorentsen, R. H., Jonas Heilskov Graversen, Caterer, N. R., Thogersen, H. C., Etzerodt, M. |
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Binding Sites
Base Sequence Sequence Homology Amino Acid Heparin Molecular Sequence Data Plasminogen Blood Proteins Exons Chromatography Affinity Recombinant Proteins Kinetics Mice Amino Acid Substitution Lectins Mutagenesis Site-Directed Animals Humans Calcium Lectins C-Type Amino Acid Sequence Sequence Alignment Research Article |
| Zdroj: | University of Southern Denmark Lorentsen, R H, Graversen, J H, Caterer, N R, Thøgersen, H C & Etzerodt, M 2000, ' The heparin-binding site in tetranectin is located in the N-terminal region and binding does not involve the carbohydrate recognition domain ', Biochem. J., vol. 347, pp. 83-87 . |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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