Backbone resonance assignments of the C2 domain of coagulation factor VIII

Kristin M. Nuzzio, David B. Cullinan, Valerie A. Novakovic, John M. Boettcher, Chad M. Rienstra, Gary E. Gilbert, James D. Baleja

Research output: Contribution to journalArticlepeer-review

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 languageEnglish (US)
Pages (from-to)31-34
Number of pages4
JournalBiomolecular NMR Assignments
Volume7
Issue number1
DOIs
StatePublished - Apr 2013

Keywords

  • Blood coagulation
  • C2 discoidin-like domain
  • FVIII
  • Membrane-associated protein

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

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