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A hydrophobic patch (PLVIVG; 1481–1486) in the B‐domain of factor V‐short is crucial for its synergistic TFPIα‐cofactor activity with protein S and for the formation of the FXa‐inhibitory complex comprising FV‐short, TFPIα, and protein S

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Factor V‐short (FV756‐1458) is a natural splice variant functioning in synergy with protein S as tissue factor pathway inhibitor alpha (TFPIα)–cofactor in inhibition of factor Xa (FXa). An exposed acid… Click to show full abstract

Factor V‐short (FV756‐1458) is a natural splice variant functioning in synergy with protein S as tissue factor pathway inhibitor alpha (TFPIα)–cofactor in inhibition of factor Xa (FXa). An exposed acid region (AR2; 1493–1537) in the B domain binds TFPIα. The preAR2 (1458–1492) is crucial for the synergistic TFPIα–cofactor activity between FV‐short and protein S and for assembly of a trimolecular FXa‐inhibitory complex among FV‐short, protein S, and TFPIα.

Keywords: factor short; tfpi cofactor; tfpi; protein

Journal Title: Journal of Thrombosis and Haemostasis
Year Published: 2022

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