1DEC

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

1DEC の概要

• エントリーDOI: 10.2210/pdb1dec/pdb
• 分子名称: DECORSIN (1 entity in total)
• 機能のキーワード: blood coagulation
• 由来する生物種: Macrobdella decora (North American leech)
• 細胞内の位置: Secreted: P17350
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4388.87

構造登録者

Krezel, A.M.,Wagner, G.,Seymour-Ulmer, J.,Lazarus, R.A. (登録日: 1994-05-17, 公開日: 1994-08-31, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

SOLUTION NMR