Citation

Structure, function and evolution of multidomain proteins

Cyrus Vogel, Matthew Bashton, Nigel D. Kerrison, Cyrus Chothia, Sarah A. Teichmann

Current Opinion in Structural Biology (2004)

TL;DR

Approximately 4,000 well-characterized domain families exist

This paper establishes the foundational understanding of protein domain modularity that the chapter uses to introduce biological modularity principles. The authors show that approximately 4,000 domain families have been recombined to produce hundreds of thousands of distinct proteins.

The research demonstrates how modular building blocks enable combinatorial evolution - rather than nature 'inventing' each protein function independently, a relatively small toolkit of domains has been recombined in various ways. This provides the biological foundation for understanding how organizations can similarly build diverse capabilities from standardized components.

Key Findings from Vogel et al. (2004)

  • Approximately 4,000 well-characterized domain families exist
  • Domains recombine to produce hundreds of thousands of distinct proteins
  • The same domain architecture appears across functionally diverse proteins
  • Combinatorial evolution is more efficient than de novo protein invention

Related Mechanisms for Structure, function and evolution of multidomain proteins

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