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Title
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Crystal structure of the factor XI zymogen reveals a pathway for transactivation.
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Authors
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E.Papagrigoriou,
P.A.McEwan,
P.N.Walsh,
J.Emsley.
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Ref.
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Nat Struct Mol Biol, 2006,
13,
557-558.
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PubMed id
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Abstract
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Factor XI (FXI), a coagulation protein essential to normal hemostasis,
circulates as a disulfide-linked dimer. Here we report the full-length FXI
zymogen crystal structure, revealing that the protease and four apple domains
assemble into a unique 'cup and saucer' architecture. The structure shows that
the thrombin and platelet glycoprotein Ib binding sites are remote within the
monomer but lie in close proximity across the dimer, suggesting a
transactivation mechanism.
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