[From structure to function: new developments in the interaction of coagulation factor Ⅴ with tissue factor pathway inhibitor α].
- 1Department of Hematology, the Second Hospital of Shanxi Medical University, Center for Shanxi Medical University and Tumor of the Hematopoietic and Lymphoid Tissues Diseases, Shanxi Provincial Key Laboratory for Molecular Diagnosis and Treatment of Hematological Diseases, Taiyuan 030001, China.
Abstract
The interaction between coagulation factor Ⅴ (FⅤ) and tissue factor pathway inhibitor alpha (TFPIα) is a central regulator of hemostatic balance. The acidic region (AR2) of the FⅤ B domain interacts with either its basic region (BR) or the basic C-terminal tail of TFPIα, modulating FⅤ activity. Recent cryo-electron microscopy studies have resolved the high-resolution structures of FⅤ-short and full-length FⅤ, revealing that AR2 forms a negatively charged hydrophobic platform that mediates BR or TFPIα binding. These insights confirm the BR-AR2 interaction as crucial for maintaining FⅤ in its inactive state and clarify the molecular basis of FⅤ-related disorders, highlighting the FⅤ-TFPIα interface as a promising therapeutic target for bleeding and thrombotic diseases.
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BibTeX
@article{li2026from,
title = {{[From structure to function: new developments in the interaction of coagulation factor Ⅴ with tissue factor pathway inhibitor α].}},
author = {B X Li and L H Yang and G Wang},
journal = {Zhonghua xue ye xue za zhi = Zhonghua xueyexue zazhi},
year = {2026},
month = aug,
doi = {10.3760/cma.j.cn121090-20251112-00523},
url = {https://europepmc.org/article/MED/42851187},
note = {CC BY},
}
RIS
TY - JOUR
TI - [From structure to function: new developments in the interaction of coagulation factor Ⅴ with tissue factor pathway inhibitor α].
AU - B X Li
AU - L H Yang
AU - G Wang
PY - 2026
DA - 2026/08/01
JO - Zhonghua xue ye xue za zhi = Zhonghua xueyexue zazhi
DO - 10.3760/cma.j.cn121090-20251112-00523
UR - https://europepmc.org/article/MED/42851187
AB - The interaction between coagulation factor Ⅴ (FⅤ) and tissue factor pathway inhibitor alpha (TFPIα) is a central regulator of hemostatic balance. The acidic region (AR2) of the FⅤ B domain interacts with either its basic region (BR) or the basic C-terminal tail of TFPIα, modulating FⅤ activity. Recent cryo-electron microscopy studies have resolved the high-resolution structures of FⅤ-short and full-length FⅤ, revealing that AR2 forms a negatively charged hydrophobic platform that mediates BR or TFPIα binding. These insights confirm the BR-AR2 interaction as crucial for maintaining FⅤ in its inactive state and clarify the molecular basis of FⅤ-related disorders, highlighting the FⅤ-TFPIα interface as a promising therapeutic target for bleeding and thrombotic diseases.
SN - 0253-2727
SN - 2707-9740
ER -