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Related Experiment Videos

Antithrombin III: structural and functional aspects.

L Mourey1, J P Samama, M Delarue

  • 1Laboratoire de Cristallographie Biologique, IBMC du CNRS, Strasbourg, France.

Biochimie
|August 1, 1990
PubMed
Summary
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Antithrombin III, a key protein in blood clotting, has had its cleaved structure determined. This reveals its similarity to other serpins and describes its heparin binding site.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Hematology

Background:

  • Antithrombin III is a vital plasma glycoprotein regulating blood coagulation.
  • It functions by inhibiting thrombin within the coagulation cascade.
  • Its activity is modulated by the polysaccharide heparin.

Purpose of the Study:

  • To determine the X-ray structure of the cleaved form of antithrombin III.
  • To describe the heparin binding site on antithrombin III.
  • To discuss the structural transition between native and cleaved antithrombin III.

Main Methods:

  • X-ray crystallography
  • Structure determination and refinement to 3.2 A resolution.

Main Results:

Related Experiment Videos

  • The X-ray structure of cleaved antithrombin III was determined.
  • The overall topology is similar to alpha 1-antitrypsin, a related serpin.
  • The heparin binding site was identified and described.

Conclusions:

  • The determined structure provides insights into antithrombin III function.
  • Structural similarity to other serpins is confirmed.
  • Understanding the heparin binding site is crucial for its biological activity.