Work

[From structure to function: new developments in the interaction of coagulation factor Ⅴ with tissue factor pathway inhibitor α].

Year: 2026

Type: review

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.

Source: PubMed Central

DOI: 10.3760/cma.j.cn121090-20251112-00523

Authors: B X Li, L H Yang, G Wang

Institutions: Shanxi Medical University, Second Hospital of Shanxi Medical University

Language: Chinese

Topic: Blood Coagulation and Thrombosis Mechanisms

Subfield: Hematology

Field: Medicine

Domain: Health Sciences

SDG: Good health and well-being

Open Access status: green

OpenAlex ID: W7221184139