Crystal structure of the factor XI zymogen reveals a pathway for transactivation.
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.
Papagrigoriou
Evangelos
E
Centre for Biomolecular Sciences, School of Pharmacy, University of Nottingham, Nottingham, NG72RD, UK.
McEwan
Paul A
PA
Walsh
Peter N
PN
Emsley
Jonas
J
D018360:Crystallography, X-Ray; D004792:Enzyme Precursors / Q000737:chemistry*; D005172:Factor XI / Q000737:chemistry*; D008958:Models, Molecular; D015533:Transcriptional Activation
D004792:Enzyme Precursors; D005172:Factor XI