Primary structure of bovine vitamin K-dependent protein S

Summary, in English

Protein S is a vitamin K-dependent plasma protein that functions as a cofactor to activated protein C in the inactivation of coagulation factors Va and VIIIa. The nucleotide sequence of a full-length cDNA clone, obtained from a bovine liver library, was determined and the amino acid sequence was deduced. In addition, 95% of the structure was determined by protein sequencing. Protein S consists of 634 amino acids in a single polypeptide chain and has one asparagine-linked carbohydrate side chain. The cDNA sequence showed that the protein has a leader sequence, 41 amino acid residues long. The amino-terminal part of the molecule containing gamma-carboxyglutamic acid is followed by a region, residues 42-75, with two peptide bonds that are very sensitive to cleavage by thrombin. Residues 76-244 have four cysteinerich repeat sequences, each about 40 residues long, that are homologous to the precursor of mouse epidermal growth factor. In contrast to the other vitamin K-dependent plasma proteins, the carboxyl-terminal part of protein S is not homologous to the serine proteases.

• Författare: Björn Dahlbäck; Åke Lundwall; Johan Stenflo
• Avdelning/ar: Klinisk kemi, Malmö
• Publiceringsår: 1986
• Språk: Engelska
• Sidor: 203-4199
• Publikation/Tidskrift/Serie: Proc Natl Acad Sci U S A
• Volym: 83
• Issue: 12
• Länkar: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2940598
• Dokumenttyp: Artikel i tidskrift
• Ämne: Medicinal Chemistry
• Nyckelord: *Glycoproteins/genetics; Disulfides; DNA/genetics; Molecular; Cloning; Cattle; *Blood Coagulation Factors/genetics; Amino Acid Sequence; Animals; Protein Conformation; Protein S; Research Support; Non-U.S. Gov't; Vitamin K
• Status: Published
• Forskningsgrupp: Clinical Chemistry, Malmö