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Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes

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Published on: June 3, 2014

Crystal structure of prethrombin-1.

Zhiwei Chen¹, Leslie A Pelc, Enrico Di Cera

¹Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, Saint Louis, MO 63104, USA.

Proceedings of the National Academy of Sciences of the United States of America

|October 27, 2010

Summary

The crystal structure of prethrombin-1 reveals its zymogen form has conformational plasticity. This finding impacts understanding of prothrombin activation and the conversion of zymogens to proteases.

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Area of Science:

Biochemistry
Structural Biology
Proteolysis

Background:

Prothrombin is the inactive precursor to thrombin, a key enzyme in blood clotting.
The three-dimensional structure of prothrombin has remained elusive.
Prethrombin-1 is a variant lacking N-terminal residues, offering a glimpse into the prothrombin structure.

Purpose of the Study:

To determine the X-ray crystal structure of prethrombin-1.
To compare the structure of prethrombin-1 to its active form, meizothrombin desF1.
To elucidate the conformational changes during prothrombin activation.

Main Methods:

X-ray crystallography
Structure determination at 2.2-Å resolution
Conformational analysis and comparison

Main Results:

The prethrombin-1 structure differs significantly from meizothrombin desF1.
Fragment 2 in prethrombin-1 is rotated, with limited interaction with the B chain.
The active site of prethrombin-1 is occluded by a helical autolysis loop, with key residues W148 and W215 positioned closely.

Conclusions:

Zymogen prothrombin exhibits significant conformational plasticity, similar to its active form.
The structural findings provide insights into the mechanism of prothrombin activation.
The study sheds light on the zymogen-to-protease conversion process in trypsin-like proteases.