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Curr Opin Struct Biol. 2019 Jun;56:155-163. doi: 10.1016/j.sbi.2019.03.009. Epub 2019 Apr 17.

The functional importance of structure in unstructured protein regions.

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1
Conway Institute of Biomolecular & Biomedical Research, University College Dublin, Belfield, Dublin 4, Ireland; Division of Cancer Biology, The Institute of Cancer Research, 237 Fulham Road, London SW3 6JB, UK. Electronic address: norman.davey@icr.ac.uk.

Abstract

After two decades of research, intrinsically disordered regions (IDRs) are established as a widespread phenomenon. The growing understanding of the significant functional role of IDRs has challenged the structure-function paradigm, proving irrefutably that a stably folded structure is not a strict requirement for function. Nonetheless, (un)structure-function relationships remain at the core of IDR-mediated interactions. An IDR can populate a continuously transitioning continuum of structural conformations from fully disordered to stable globular states. In these ensembles, only subsets of conformations are binding competent, with intramolecular IDR contacts serving as important intermolecular binding determinants. Here, we review our current understanding of different types of intramolecular IDR interactions, their effects on IDR complex formation and their modes of biological regulation.

PMID:
31003202
DOI:
10.1016/j.sbi.2019.03.009
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