Open AccessBackbone resonance assignments of the C2 domain of coagulation factor VIII
Author(s) -
Kristin M. Nuzzio,
David B. Cullinan,
Valerie A. Novakovic,
John M. Boettcher,
Chad M. Rienstra,
Gary E. Gilbert,
James D. Baleja
Publication year - 2012
Publication title -
biomolecular nmr assignments
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.359
H-Index - 16
eISSN - 1874-2718
pISSN - 1874-270X
DOI - 10.1007/s12104-012-9370-5
Subject(s) - coagulation , domain (mathematical analysis) , resonance (particle physics) , factor (programming language) , chemistry , nuclear magnetic resonance , physics , computer science , medicine , mathematics , atomic physics , mathematical analysis , programming language
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, (1)H, (13)C, and (15)N 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.