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Actin-binding protein complexes at atomic resolution

P J McLaughlin1, A G Weeds

  • 1MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.

Annual Review of Biophysics and Biomolecular Structure
|January 1, 1995
PubMed
Summary
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This review examines actin

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Actin is a crucial protein involved in cellular structure and motility.
  • Monomer-binding proteins regulate actin dynamics by interacting with actin monomers.
  • Understanding these interactions is key to deciphering cellular processes.

Purpose of the Study:

  • To review and analyze the structural basis of actin complex formation with specific monomer-binding proteins.
  • To compare the binding interfaces and conservation patterns of these complexes.
  • To identify conserved structural features and differences in actin-binding proteins.

Main Methods:

  • Structural analysis of actin complexes.
  • Comparison of binding site residues and conservation patterns.

Related Experiment Videos

  • Review of existing crystallographic and biochemical data.

    • Main Results:

    • Three distinct actin-monomer-binding protein structures (DNase I, gelsolin segment 1, profilin) were analyzed.
    • Binding sites are often discontinuous and lack conserved hydrogen-bonding residues.
    • Conserved residues in gelsolin and profilin relate to their structural folds, not solely actin binding.
    • Actin binding surfaces for segment 1 and profilin differ but show peripheral overlap.
    • No unique or extreme features characterize these actin-binding surfaces compared to other globular proteins.

    Conclusions:

    • Actin's interactions with monomer-binding proteins are structurally diverse.
    • Conservation patterns highlight protein fold stability over specific binding site residues.
    • The structural basis for actin regulation involves complex, non-uniform binding interfaces.