The functional importance of structure in unstructured protein regions.
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ICR Authors
Authors
Davey, NE
Document Type
Journal Article
Date
2019-06-01
Date Accepted
2019-03-07
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.
Citation
Current opinion in structural biology, 2019, 56 pp. 155 - 163
Source Title
Publisher
CURRENT BIOLOGY LTD
ISSN
0959-440X
eISSN
1879-033X