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The structure and function of protein modules.

I D Campbell1, M Baron

  • 1Department of Biochemistry, University of Oxford, U.K.

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
|May 29, 1991
PubMed
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Protein modules, often formed by exon shuffling, are key to protein function and specificity in multicellular organisms. Studying their structure via nuclear magnetic resonance and mutagenesis reveals critical functional insights.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Multicellular organism proteins evolve via exon shuffling, deletion, and duplication, often yielding autonomously folding modules.
  • Extracellular enzymes like serine proteases exhibit modular structures crucial for protein-protein interactions and specificity.
  • Limited structural data necessitates novel strategies for understanding protein module structure and function.

Purpose of the Study:

  • To develop and apply a new strategy for investigating the structure and function of protein modules.
  • To elucidate the structural basis of module function in key extracellular proteins.

Main Methods:

  • Production of individual protein modules using protein expression techniques.
  • High-resolution structure determination via nuclear magnetic resonance (NMR).

Related Experiment Videos

  • Identification of functional regions using site-directed mutagenesis and biological assays.

    • Main Results:

    • Structures of key modules, including the growth factor, fibronectin type 1, and complement modules, were determined.
    • Functional patches on these modules were identified.

    Conclusions:

    • The strategy of producing, structuring, and functionally assaying individual modules is effective for studying complex proteins.
    • Understanding protein modules provides insights into the function of enzymes like factor IX and tissue plasminogen activator.