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Related Experiment Videos

Kringle-kringle interactions in multimer kringle structures

K Padmanabhan1, T P Wu, K G Ravichandran

  • 1Department of Chemistry, Michigan State University, East Lansing 48824.

Protein Science : a Publication of the Protein Society
|June 1, 1994
PubMed
Summary
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The crystal structures of human plasminogen kringle 4 (PGK4) and tissue plasminogen activator kringle 2 (t-PAK2) reveal novel kringle-kringle interactions and electrostatic binding at lysine sites, crucial for protein assembly and function.

Area of Science:

  • Structural biology
  • Biochemistry
  • Protein crystallography

Background:

  • Kringle domains are conserved protein modules found in various proteins, including plasminogen and tissue plasminogen activator.
  • Understanding the structural basis of kringle-kringle interactions is essential for elucidating the function of multikringle proteins.

Purpose of the Study:

  • To determine and refine the crystal structures of human plasminogen kringle 4 (PGK4) and tissue plasminogen activator kringle 2 (t-PAK2).
  • To investigate the nature of kringle-kringle interactions and their potential functional implications.

Main Methods:

  • Molecular replacement and X-PLOR refinement were used to solve and refine the crystal structures.
  • Restrained least-squares methods and PROFFT were employed for structure refinement.

Related Experiment Videos

  • Analysis of noncrystallographic symmetry and intermolecular interactions was performed.

    • Main Results:

    • The crystal structure of monoclinic human plasminogen kringle 4 (PGK4) was solved at 2.25 A resolution.
    • The refined structure of tissue plasminogen activator kringle 2 (t-PAK2) was obtained at 2.38 A resolution.
    • Both structures exhibit noncrystallographic symmetry and reveal extensive kringle-kringle interactions, including electrostatic interactions at lysine binding sites.

    Conclusions:

    • Kringle-kringle interactions, mediated by noncrystallographic symmetry, are prevalent in multikringle proteins.
    • Electrostatic interactions involving lysine binding sites play a significant role in these associations.
    • These findings provide insights into the assembly and function of proteins containing multiple kringle domains.