1dec

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

spinqualitylabelsall models 1dec Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1dec is a 1 chain structure with sequence from Macrobdella decora. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 25 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DECO_MACDE Inhibits fibrinogen interaction with platelet receptors expressed on glycoprotein IIb-IIIa complex. May prevent blood from clotting during either feeding and/or storage of ingested blood. Publication Abstract from PubMed 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. Structure of the RGD protein decorsin: conserved motif and distinct function in leech proteins that affect blood clotting.,Krezel AM, Wagner G, Seymour-Ulmer J, Lazarus RA Science. 1994 Jun 24;264(5167):1944-7. PMID:8009227 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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