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Related Experiment Videos

The PH superfold: a structural scaffold for multiple functions.

N Blomberg1, E Baraldi, M Nilges

  • 1European Molecular Biology Laboratory, Meyerhofstrasse 1, Postfach 10.2209, D-690 12 Heidelberg, Germany.

Trends in Biochemical Sciences
|November 5, 1999
PubMed
Summary
This summary is machine-generated.

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Pleckstrin homology (PH) domains are conserved protein modules regulating cellular pathways by binding to lipids or proteins. Their structural similarity suggests a common PH superfold, crucial for protein localization and function.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Pleckstrin homology (PH) domains are conserved protein modules involved in cellular regulatory pathways.
  • These domains exhibit a conserved fold, suggesting a stable PH superfold across different protein families.
  • PH domains typically function as regulated membrane-binding modules.

Purpose of the Study:

  • To highlight the structural conservation and functional significance of Pleckstrin homology domains.
  • To explore the concept of a PH superfold and its implications.
  • To differentiate the ligand-binding specificities of PH domains and similar folds.

Main Methods:

  • Structural analysis of Pleckstrin homology domains.
  • Comparative analysis of protein domain families.

Related Experiment Videos

  • Literature review on protein-protein and protein-lipid interactions.

    • Main Results:

    • PH domains share a conserved structure, indicating a common PH superfold.
    • PH domains bind to inositol lipids, mediating protein targeting.
    • Similar folds, like phosphotyrosine binding domains, recognize protein ligands.

    Conclusions:

    • The PH superfold is a stable structural motif with diverse functional roles.
    • PH domains are key regulators of protein localization through lipid binding.
    • Structural homology can extend across proteins with different sequence identities and ligand specificities.