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Related Experiment Videos

Two non-proline cis peptide bonds may be important for factor XIII function

M S Weiss1, H J Metzner, R Hilgenfeld

  • 1Institute of Molecular Biotechnology, Department of Structural Biology and Crystallography, Jena, Germany.

FEBS Letters
|March 27, 1998
PubMed
Summary
This summary is machine-generated.

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The structure of human cellular factor XIII zymogen was determined, revealing two non-proline cis peptide bonds. These findings may be crucial for understanding factor XIII

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Factor XIII is a transglutaminase crucial for blood coagulation and wound healing.
  • Understanding the three-dimensional structure of factor XIII zymogen is essential for elucidating its activation mechanism and function.

Purpose of the Study:

  • To determine the crystal structure of recombinant human cellular factor XIII zymogen.
  • To identify and characterize any unusual peptide bond conformations, such as cis peptide bonds.
  • To discuss the potential functional implications of these structural features for factor XIII activity.

Main Methods:

  • Recombinant expression and purification of human cellular factor XIII zymogen.
  • X-ray crystallography to solve the protein structure.

Related Experiment Videos

  • Structure refinement and analysis to identify key structural features.

    • Main Results:

    • The monoclinic crystal form of recombinant human cellular factor XIII zymogen was successfully solved and refined to 2.1 A resolution.
    • Two non-proline cis peptide bonds were identified: one near the active site (Arg310-Tyr311) and another at the dimerization interface (Gln425-Phe426).

    Conclusions:

    • The determined structure provides atomic-level insights into the factor XIII zymogen conformation.
    • The presence and location of cis peptide bonds suggest a role in regulating factor XIII activation and/or dimerization.
    • Further studies are warranted to fully elucidate the functional significance of these cis peptide bonds in factor XIII function.