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Treble clef finger--a functionally diverse zinc-binding structural motif.

N V Grishin1

  • 1Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9050, USA. grishin@chop.swmed.edu

Nucleic Acids Research
|April 9, 2001
PubMed
Summary
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Researchers discovered a common structural motif, the treble clef finger, in small metal-binding proteins. This finding unifies distinct protein folds and reveals versatile functions for this zinc-binding domain.

Area of Science:

  • Structural biology
  • Protein science
  • Bioinformatics

Background:

  • Detecting similarities in small proteins is challenging, leading to overlooked connections.
  • Existing classifications (SCOP) may not fully capture evolutionary or structural relationships among metal-binding proteins.

Purpose of the Study:

  • To identify and characterize a common structural motif in small metal-binding proteins.
  • To propose a unification of distinct protein folds based on shared structural elements.
  • To explore the functional versatility of the identified motif.

Main Methods:

  • Comparative analysis of protein structures and sequences.
  • Identification of conserved structural domains and motifs.
  • Classification and unification of protein folds.

Related Experiment Videos

Main Results:

  • A common structural motif, the "treble clef finger," was identified in various metal-binding proteins.
  • This motif, 25-45 residues long and centered around a zinc ion, forms the structural core.
  • Seven distinct SCOP folds across two protein classes were unified based on the treble clef motif.
  • The motif is present in diverse proteins including ribosomal proteins, RING fingers, and kinases, demonstrating broad applicability.

Conclusions:

  • The treble clef finger represents a distinct structural fold with significant functional versatility.
  • This motif is a major group within zinc fingers, capable of diverse metal binding and functions.
  • Unification of protein folds based on such motifs enhances our understanding of protein evolution and function.