The functional importance of structure in unstructured protein regions.
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Date
2019-06-01ICR Author
Author
Davey, NE
Type
Journal Article
Metadata
Show full item recordAbstract
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.
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Subject
Protein Structure, Quaternary
Intrinsically Disordered Proteins
Language
eng
Date accepted
2019-03-07
License start date
2019-06
Citation
Current opinion in structural biology, 2019, 56 pp. 155 - 163
Publisher
CURRENT BIOLOGY LTD