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Collagens as multidomain proteins.

M van der Rest1, R Garrone

  • 1Institute of Biology and Chemistry of Proteins (CNRS-UPR 412), Lyon, France.

Biochimie
|June 1, 1990
PubMed
Summary
This summary is machine-generated.

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Collagen-like proteins feature triple helical domains crucial for structure and function. These domains, varying in size, enable diverse molecular assemblies and offer potential for protein engineering.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Engineering

Background:

  • The number of known proteins with collagen-like triple helical domains is rapidly expanding.
  • These domains function as molecular rods, separating non-helical domains and facilitating lateral molecular interactions.

Purpose of the Study:

  • To discuss the structure and function of recently discovered collagens.
  • To explore the diverse roles of triple helical and non-triple helical domains in collagenous proteins.

Main Methods:

  • Analysis of primary structure to predict triple helix formation.
  • Examination of domain organization and sizes in various collagenous proteins.

Main Results:

  • Triple helical domains range from 33 to over 1,000 amino acids, influencing fibril formation and molecular aggregation.

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  • Non-triple helical domains vary in size, providing structural flexibility, proteolytic cleavage sites, and glycosaminoglycan attachment points.

    • Conclusions:

    • Collagen-like molecules exhibit diverse domain architectures, enabling varied functions and supramolecular assemblies.
    • The controlled in vitro assembly of collagen-like molecules presents significant opportunities for protein engineering applications.