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SH3-like fold proteins are structurally conserved and functionally divergent.

K V Radha Kishan1, Vishal Agrawal

  • 1Institute of Microbial Technology, Sector 39-A, Chandigarh 160 036, India. kishan@imtech.res.in

Current Protein & Peptide Science
|April 28, 2005
PubMed
Summary

Many unrelated protein sequences share similar folds due to limited folding space. SH3-like folds exhibit diverse functions through loop modulation, primarily on one side of a beta-sheet, enabling various ligand bindings.

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Area of Science:

  • Structural Biology
  • Protein Science
  • Bioinformatics

Background:

  • Limited protein sequence space leads to convergent evolution of similar protein folds.
  • Databases like SCOP and CATH classify protein folds but lack in-depth functional analysis.
  • Understanding the functional implications of protein fold similarity is crucial.

Purpose of the Study:

  • To analyze the structural and functional characteristics of unique SH3-like protein folds.
  • To investigate how SH3-like folds perform diverse functions.
  • To identify conserved regions within SH3-like proteins.

Main Methods:

  • Analysis of approximately twenty unique SH3-like folded proteins.
  • Examination of protein structural environments.

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  • Assessment of functional characteristics and ligand-binding capabilities.

    • Main Results:

    • SH3-like folds can perform various functions by modulating their loops.
    • The functional region is typically localized to one side of a beta-sheet, supported by key loops.
    • Functions range from oligonucleotide and peptide binding to other ligand interactions.
    • Sequence similarity among SH3-like proteins is mainly confined to beta-strand regions.

    Conclusions:

    • Protein fold similarity is a significant factor in functional diversity.
    • Loop regions play a critical role in determining the specific functions of SH3-like folds.
    • SH3-like folds represent a versatile structural motif capable of diverse molecular interactions.