Structure of the RGD protein decorsin: Conserved motif and distinct function in leech proteins that affect blood clotting

Andrzej M. Krezel, Gerhard Wagner, Jana Seymour-Ulmer, Robert A. Lazarus

Research output: Contribution to journalArticle

129 Scopus citations

Abstract

The structure of the leech protein decorsin, a potent 39-residue antagonist of glycoprotein Mb-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.

Original languageEnglish
Pages (from-to)1944-1947
Number of pages4
JournalScience
Volume264
Issue number5167
DOIs
StatePublished - Jan 1 1994
Externally publishedYes

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