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PDBsum entry 1dec
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Blood coagulation
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PDB id
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1dec
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References listed in PDB file
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Key reference
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Title
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Structure of the rgd protein decorsin: conserved motif and distinct function in leech proteins that affect blood clotting.
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Authors
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A.M.Krezel,
G.Wagner,
J.Seymour-Ulmer,
R.A.Lazarus.
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Ref.
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Science, 1994,
264,
1944-1947.
[DOI no: ]
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PubMed id
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Abstract
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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.
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