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Related Experiment Videos

Does this have a familiar RING?

A J Saurin1, K L Borden, M N Boddy

  • 1Protein Structure Laboratory, Imperial Cancer Research Fund, London, UK.

Trends in Biochemical Sciences
|June 1, 1996
PubMed
Summary
This summary is machine-generated.

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The RING finger, a unique zinc-binding domain in proteins, is crucial for mediating protein-protein interactions. Its specific structure and function in multi-protein complexes are key areas of ongoing research.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • The RING finger is a conserved zinc-binding domain present across diverse species, from plants to humans.
  • Its precise biological role and structural characteristics distinguish it from other zinc-finger motifs.
  • Despite its prevalence, the function of the RING finger domain remains largely uncharacterized.

Purpose of the Study:

  • To elucidate the functional significance of the RING finger domain in protein interactions.
  • To investigate the structural basis for the RING finger's role in mediating protein complex formation.

Main Methods:

  • Bioinformatic analysis of sequence homology.
  • Structural studies to determine zinc-ligation and three-dimensional structure.

Related Experiment Videos

  • Experimental investigation of protein-protein interactions involving RING finger domains.

    • Main Results:

    • The RING finger domain exhibits unique sequence and structural features compared to other zinc fingers.
    • Evidence suggests the RING finger domain mediates protein-protein interactions.
    • The domain appears to be involved in the assembly of multi-protein complexes.

    Conclusions:

    • The RING finger domain plays a significant role in protein-protein interactions and complex formation.
    • Its function may be modulated by the presence of other proteins or domains.
    • Further research is warranted to fully understand the enigmatic function of the RING finger.