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RNA-seq Analysis of Transcriptomes in Thrombin-treated and Control Human Pulmonary Microvascular Endothelial Cells

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The folding pathway of prothrombin.

Bosko M Stojanovski¹, Enrico Di Cera¹

¹Edward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St. Louis, Missouri, USA.

Journal of Thrombosis and Haemostasis : JTH

|May 22, 2026

Summary

Prothrombin folding involves domain arrangement and interdomain contacts, crucial for stabilizing its closed form. Disruptions in these contacts are linked to bleeding disorders (coagulopathies).

Keywords:

blood coagulation fluorescence resonance energy transfer protein folding prothrombin serine protease

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Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes

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Published on: June 3, 2014

Area of Science:

Biochemistry
Molecular Biology
Protein Folding Dynamics

Background:

Prothrombin is a key coagulation factor with distinct domains: γ-carboxyglutamate, kringle1, kringle2, and protease.
Interactions between these domains establish the protein's functional closed conformation.

Purpose of the Study:

To elucidate the folding process of prothrombin.
To understand how its constitutive domains and interdomain contacts are formed.

Main Methods:

Chemical denaturation was employed to study prothrombin's folding pathway.
Single molecule and ensemble spectroscopic techniques were utilized.

Main Results:

Under denaturation, prothrombin's domains separate, leading to an elongated structure.
As folding progresses, secondary and tertiary structures form, organizing hydrophobic residues and promoting domain folding.
Extensive interdomain contacts assemble to form the native state's arrangement.

Conclusions:

Correct domain folding is essential for forming interdomain contacts that stabilize prothrombin's closed conformation.
Destabilized interdomain contacts in prothrombin are implicated in the development of certain coagulopathies.