Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 13, Issue 6, Pages 557-558Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1095
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Funding
- NHLBI NIH HHS [P01 HL74124, R01 HL46213] Funding Source: Medline
- Wellcome Trust [072975] Funding Source: Medline
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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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