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Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes
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Coagulation factor XII protease domain crystal structure.

M Pathak1, P Wilmann, J Awford

  • 1Centre for Biomolecular Sciences, School of Pharmacy, University of Nottingham, Nottingham, UK.

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|January 22, 2015
PubMed
Summary
This summary is machine-generated.

Coagulation factor XII (FXII) zymogen activation and substrate recognition were investigated. The crystal structure reveals a zymogen conformation and an enlarged S1 pocket, providing a structural basis for FXII function.

Keywords:
active sitecatalytic domainfactor XIIplasma prokallikreintertiary protein structurezymogens

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Coagulation factor XII (FXII) is a serine protease crucial for kinin generation and blood coagulation.
  • FXII cleaves plasma kallikrein and coagulation factor XI (FXI) substrates.

Purpose of the Study:

  • To elucidate FXII zymogen activation mechanisms.
  • To determine the crystal structure of the FXII protease domain for substrate recognition insights.

Main Methods:

  • Characterization of recombinant FXII protease constructs.
  • Measurement of proteolytic activity using chromogenic peptide and plasma kallikrein substrates.
  • Determination of crystal structures of FXII protease domains.

Main Results:

  • FXII light chain protease exhibits weak activity compared to constructs with heavy chain remnants.
  • Crystal structures reveal a zymogen conformation with an absent oxyanion hole and atypical 70-loop.
  • An enlarged and distorted S1 pocket was observed in a second crystal form, impacting P1 Arg substrate binding.
  • Negative charge patches surround the active site cleft, potentially mediating interactions.

Conclusions:

  • The study provides the first structural insights into FXII substrate recognition.
  • These findings offer a structural basis for understanding FXII zymogen activation.