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Nat Struct Mol Biol. 2006 Jun;13(6):557-8. Epub 2006 May 14.

Crystal structure of the factor XI zymogen reveals a pathway for transactivation.

Author information

1
Centre for Biomolecular Sciences, School of Pharmacy, University of Nottingham, Nottingham, NG72RD, UK.

Abstract

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.

PMID:
16699514
DOI:
10.1038/nsmb1095
[Indexed for MEDLINE]

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