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Issue 1, 2012
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Aromatic residues link binding and function of intrinsically disordered proteins

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Abstract

We have searched for intermolecular aromatic pairs in 77 protein–protein complexes of intrinsically disordered proteins (IDPs) to understand the role of π–π interactions in proteinprotein interactions involving IDPs. We found that 40% of the complexes possess at least one intermolecular pair of aromatic residues. Analysis of composition, characteristics, location and the contribution to the free energy of binding showed that π–π interactions substantially contribute to binding by working as anchor residues, conformational locks, and ready-made recognition motifs required for specific binding. By using available experimental data we show that π–π interactions play a variety of roles that link binding of IDPs and their function in the cell. The results presented in this study pave the way to understand in atomic detail the inner workings of IDPs interaction networks.

Graphical abstract: Aromatic residues link binding and function of intrinsically disordered proteins

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Publication details

The article was received on 15 Jun 2011, accepted on 29 Jul 2011 and first published on 24 Aug 2011


Article type: Paper
DOI: 10.1039/C1MB05239J
Mol. BioSyst., 2012,8, 237-246

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    Aromatic residues link binding and function of intrinsically disordered proteins

    L. M. Espinoza-Fonseca, Mol. BioSyst., 2012, 8, 237
    DOI: 10.1039/C1MB05239J

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