Coil conversion to [beta]-strand induced by dimerization

Johanna Laibe, Aaron Caffrey, Melanie Broutin, Solene Guiglion, Barbara Pierscionek, Jean Christophe Nebel

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Most molecular processes in living organisms rely on protein-protein interactions, many of which are mediated by β-sheet interfaces; this study investigates the formation of β-sheet interfaces through the conversion of coils into β-strands. Following an exhaustive search in the Protein Data Bank, the corresponding structural dimorphic fragments were extracted, characterised and analysed. Their short strand lengths and specific amino acid profiles indicate that dimorphic β-strand interfaces are likely to be less stable than standard ones and could even convert to coil interfaces if their environment changes. Moreover, the construction of a simple classifier able to discriminate between the sequences of dimorphic and standard β-strand interfaces suggests that the nature of those dimorphic sequences could be predicted, providing a novel means of identifying proteins capable of forming dimers.
    Original languageEnglish
    Pages (from-to)1221-1230
    JournalProteins: Structure, Function and Bioinformatics
    Volume86
    Issue number12
    Early online date18 Jul 2018
    DOIs
    Publication statusPublished - 31 Dec 2018

    Keywords

    • Biological sciences
    • dimorphic sequences
    • intermolecular β-strand interfaces
    • protein conformational change
    • protein dimerisation
    • protein structure
    • protein-protein interaction

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