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Related Experiment Video

Updated: Jun 27, 2026

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
13:34

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD

Published on: December 30, 2016

High quality structure of cleaved PAI-1-stab.

M Dewilde1, S V Strelkov, A Rabijns

  • 1Katholieke Universiteit Leuven, Belgium.

Journal of Structural Biology
|December 9, 2008
PubMed
Summary

We determined the crystal structure of a stabilized plasminogen activator inhibitor-1 (PAI-1) variant, revealing a cleavage in its reactive center loop. This high-quality structure offers new insights into PAI-1

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Mechanisms

Background:

  • Plasminogen activator inhibitor-1 (PAI-1) is a key regulator of fibrinolysis.
  • Understanding PAI-1's structure is crucial for developing therapeutic strategies.

Purpose of the Study:

  • To determine the high-resolution crystal structure of a stabilized PAI-1 variant (PAI-1-stab).
  • To elucidate the structural basis of PAI-1 cleavage and its mechanism of action.

Main Methods:

  • X-ray crystallography
  • Structure comparison
  • Analysis of stabilizing mutations

Main Results:

  • Reported the crystal structure of PAI-1-stab with a cleaved reactive center loop.

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Related Experiment Videos

Last Updated: Jun 27, 2026

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
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A High-Throughput Luciferase Assay to Evaluate Proteolysis of the Single-Turnover Protease PCSK9

Published on: August 28, 2018

  • The new structure is of superior quality compared to previous PAI-1 mutant structures.
  • Detailed comparison with active PAI-1-stab and a cleaved mutant (PAI-1-A335P) was performed.

    • Conclusions:

    • The structural data provide significant insights into PAI-1's working mechanism.
    • The study explains the functional role of specific stabilizing mutations in PAI-1.