In molecular biology, ornatin is a potent glycoprotein IIb-IIIa (GP IIb-IIIa) antagonist and platelet aggregation inhibitor isolated from Placobdella ornata (Turtle leech).[1] The protein is 41-52 amino acids in length and contains the RGD recognition motif common in adhesion proteins, and 6 conserved cysteine residues. These form three disulphide bonds, which are required for activity.[2] The sequences of ornatin B, C, D and E are highly similar, while A2 and A3 are less similar, lacking the N-terminal 9 residues. Ornatins share ~40% identity with decorsin, a GP IIb-IIIa antagonist isolated from the leech (Macrobdella decora).[1]
| Ornatin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Ornatin | ||||||||
| Pfam | PF02088 | ||||||||
| InterPro | IPR002463 | ||||||||
| |||||||||
References edit
- ^ a b Mazur P, Henzel WJ, Seymour JL, Lazarus RA (December 1991). "Ornatins: potent glycoprotein IIb-IIIa antagonists and platelet aggregation inhibitors from the leech Placobdella ornata". Eur. J. Biochem. 202 (3): 1073–82. doi:10.1111/j.1432-1033.1991.tb16472.x. PMID 1765068.
- ^ Mazur P, Dennis MS, Seymour JL, Lazarus RA (1993). "Expression, purification, and characterization of recombinant ornatin E, a potent glycoprotein IIb-IIIa antagonist". Protein Expr Purif. 4 (4): 282–9. doi:10.1006/prep.1993.1036. PMID 8374297.