Abstract
Factor VIII (FVIII, other clotting factors are named similarly) is a glycoprotein that circulates in the plasma bound to von Willebrand factor. During the blood coagulation cascade, activated FVIII (FVIIIa) binds to FIXa and activates FX in the presence of calcium ions and phospholipid membranes. The C1 and C2 domains mediate membrane binding that is essential for activation of the FVIIIa-FIXa complex. Here, 1H, 13C, and 15N backbone chemical shift assignments are reported for the C2 domain of FVIII, including assignments for the residues in solvent-exposed loops. The NMR resonance assignments, along with further structural studies of membrane-bound FVIII, will advance understanding of blood-clotting protein interactions.
Original language | English (US) |
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Pages (from-to) | 31-34 |
Number of pages | 4 |
Journal | Biomolecular NMR Assignments |
Volume | 7 |
Issue number | 1 |
DOIs | |
State | Published - Apr 2013 |
Keywords
- Blood coagulation
- C2 discoidin-like domain
- FVIII
- Membrane-associated protein
ASJC Scopus subject areas
- Structural Biology
- Biochemistry