1DEC

STRUCTURE OF THE RGD PROTEIN DECORSIN: CONSERVED MOTIF AND DISTINCT FUNCTION IN LEECH PROTEINS THAT AFFECT BLOOD CLOTTING

Summary for 1DEC

• Entry DOI: 10.2210/pdb1dec/pdb
• Descriptor: DECORSIN (1 entity in total)
• Functional Keywords: blood coagulation
• Biological source: Macrobdella decora (North American leech)
• Cellular location: Secreted: P17350
• Total number of polymer chains: 1
• Total formula weight: 4388.87

Authors

Krezel, A.M.,Wagner, G.,Seymour-Ulmer, J.,Lazarus, R.A. (deposition date: 1994-05-17, release date: 1994-08-31, Last modification date: 2024-10-30)

Primary citation

Krezel, A.M.,Wagner, G.,Seymour-Ulmer, J.,Lazarus, R.A.
Structure of the RGD protein decorsin: conserved motif and distinct function in leech proteins that affect blood clotting.
Science, 264:1944-1947, 1994

PubMed Abstract: The structure of the leech protein decorsin, a potent 39-residue antagonist of glycoprotein IIb-IIIa and inhibitor of platelet aggregation, was determined by nuclear magnetic resonance. In contrast to other disintegrins, the Arg-Gly-Asp (RGD)-containing region of decorsin is well defined. The three-dimensional structure of decorsin is similar to that of hirudin, an anticoagulant leech protein that potently inhibits thrombin. Amino acid sequence comparisons suggest that ornatin, another glycoprotein IIb-IIIa antagonist, and antistasin, a potent Factor Xa inhibitor and anticoagulant found in leeches, share the same structural motif. Although decorsin, hirudin, and antistasin all affect the blood clotting process and appear similar in structure, their mechanisms of action and epitopes important for binding to their respective targets are distinct.

PubMed: 8009227

Experimental method

SOLUTION NMR