Assembly reflects evolution of protein complexes

Emmanuel D. Levy (), Elisabetta Boeri Erba, Carol V. Robinson () and Sarah A. Teichmann ()
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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

Nature, 2008, vol. 453, issue 7199, 1262-1265

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.

Date: 2008
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DOI: 10.1038/nature06942

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