The complex of coagulation factor VIIa (FVIIa), a trypsin-like serine protease, and membrane bound tissue factor (TF) initiates blood coagulation upon vascular injury. Binding of TF to FVIIa promotes allosteric conformational changes in the FVIIa protease domain and improves its catalytic properties. Extensive studies have revealed two putative pathways for this allosteric communication. Here we provide further details of this allosteric communication by investigating FVIIa loop swap variants containing the 170-loop of trypsin that display TF-independent enhanced activity. Using x-ray crystallography, we show that the introduced 170-loop from trypsin directly interacts with the FVIIa active-site, stabilizing segment 215-217a and activation ...
Blood coagulation factor VIIa (FVIIa) is used in the treatment of replacement therapy resistant hemo...
Blood clotting is triggered when the plasma serine protease factor VIIa binds to the cell-surface pr...
Proteolytic cleavage of the peptide bond between Arg(152) and Ile(153) converts the procoagulant pro...
<p>Tissue factor (TF)-mediated factor VII (FVII) activation and a subsequent proteolytic TF-FVIIa bi...
AbstractBackground: Coagulation factor VIIa (FVIIa) contains a Trypsin-like serine protease domain a...
Factor VIIa (EC 3.4.21.21) is a trypsin-like serine protease that plays a key role in the blood coag...
Activated Factor VII (FVIIa) is a vitamin-K-dependent serine protease that initiates blood clotting ...
Binding of factor VIIa (FVIIa) to tissue factor (TF) and the subsequent initiation of the clotting c...
AbstractIn the crystal structure of the complex between the soluble extracellular domain of tissue f...
The presence of tissue its full catalytic poten Blood coagulation factor VIIa (FVIIa) is a tryp-E-ma...
Blood clotting is a crucial step in the wound healing process. In a series of proteolytic cleavage r...
International audienceUpon binding to tissue factor, FVIIa triggers coagulation by activating vitami...
AbstractCoagulation factor VIIa (FVIIa) belongs to a family of proteases being part of the stepwise,...
Blood clotting is initiated by the two-subunit enzyme consisting of the plasma protease, factor VIIa...
Blood clotting is initiated by the two-subunit enzyme consisting of the plasma protease, factor VIIa...
Blood coagulation factor VIIa (FVIIa) is used in the treatment of replacement therapy resistant hemo...
Blood clotting is triggered when the plasma serine protease factor VIIa binds to the cell-surface pr...
Proteolytic cleavage of the peptide bond between Arg(152) and Ile(153) converts the procoagulant pro...
<p>Tissue factor (TF)-mediated factor VII (FVII) activation and a subsequent proteolytic TF-FVIIa bi...
AbstractBackground: Coagulation factor VIIa (FVIIa) contains a Trypsin-like serine protease domain a...
Factor VIIa (EC 3.4.21.21) is a trypsin-like serine protease that plays a key role in the blood coag...
Activated Factor VII (FVIIa) is a vitamin-K-dependent serine protease that initiates blood clotting ...
Binding of factor VIIa (FVIIa) to tissue factor (TF) and the subsequent initiation of the clotting c...
AbstractIn the crystal structure of the complex between the soluble extracellular domain of tissue f...
The presence of tissue its full catalytic poten Blood coagulation factor VIIa (FVIIa) is a tryp-E-ma...
Blood clotting is a crucial step in the wound healing process. In a series of proteolytic cleavage r...
International audienceUpon binding to tissue factor, FVIIa triggers coagulation by activating vitami...
AbstractCoagulation factor VIIa (FVIIa) belongs to a family of proteases being part of the stepwise,...
Blood clotting is initiated by the two-subunit enzyme consisting of the plasma protease, factor VIIa...
Blood clotting is initiated by the two-subunit enzyme consisting of the plasma protease, factor VIIa...
Blood coagulation factor VIIa (FVIIa) is used in the treatment of replacement therapy resistant hemo...
Blood clotting is triggered when the plasma serine protease factor VIIa binds to the cell-surface pr...
Proteolytic cleavage of the peptide bond between Arg(152) and Ile(153) converts the procoagulant pro...