Publication Date:
1994-06-24
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krezel, A M -- Wagner, G -- Seymour-Ulmer, J -- Lazarus, R A -- New York, N.Y. -- Science. 1994 Jun 24;264(5167):1944-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8009227" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
Hirudins/chemistry
;
Invertebrate Hormones/chemistry
;
*Leeches
;
Magnetic Resonance Spectroscopy
;
Molecular Sequence Data
;
Oligopeptides/chemistry
;
Platelet Membrane Glycoproteins/*antagonists & inhibitors
;
Protein Conformation
;
Protein Structure, Secondary
;
Proteins/*chemistry
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
