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Assembly reflects evolution of protein complexes

Author

Listed:
  • Emmanuel D. Levy

    (MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK)

  • Elisabetta Boeri Erba

    (University of Cambridge)

  • Carol V. Robinson

    (University of Cambridge)

  • Sarah A. Teichmann

    (MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK)

Abstract

Protein assembly: Products of evolution The majority of proteins tend to bind to one or several copies of themselves and assemble as 'homo-oligomeric' complexes — or homomers. Based on the known crystallographic structures of 5,000 such complexes, Levy et al. have derived plausible pathways for the emergence of ever more complex such assemblies during evolution. Using electrospray mass spectrometry, they observe that the same pathways are followed on the shorter timescale of protein assembly in vitro. Homophilic protein interactions are fundamental in biochemical processes such as allostery and the predictive method developed here should help targeting drugs to protein–protein interfaces more efficiently.

Suggested Citation

  • Emmanuel D. Levy & Elisabetta Boeri Erba & Carol V. Robinson & Sarah A. Teichmann, 2008. "Assembly reflects evolution of protein complexes," Nature, Nature, vol. 453(7199), pages 1262-1265, June.
    • Handle: RePEc:nat:nature:v:453:y:2008:i:7199:d:10.1038_nature06942
    DOI: 10.1038/nature06942
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    Cited by:

    1. Alexander S Leonard & Sebastian E Ahnert, 2019. "Evolution of interface binding strengths in simplified model of protein quaternary structure," PLOS Computational Biology, Public Library of Science, vol. 15(6), pages 1-15, June.

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