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Coagulation factor VIIa (FVIIa) is an atypical member of the trypsin family of serine proteases. It fails to attain spontaneously
its catalytically competent conformation and requires its protein cofactor tissue factor (TF) to accomplish this. Over a number
of years, this unique behaviour of FVIIa has prompted investigations of the TF-induced activation mechanism and the zymogenicity
determinants in factor VIIa. Factor VIIa has gained additional interest in the past decade because of its development into
a clinically useful haemostatic agent. Here, we present an overview of the current knowledge about the TF-induced allosteric
activation of FVIIa and the various molecular approaches to enhance the intrinsic activity and efficacy of FVIIa.
Received 18 October 2007; received after revision 12 November 2007; accepted 14 November 2007 相似文献
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