10.5061/DRYAD.33VN1
Varadi, Mihaly
Vrije Universiteit Brussel
Zsolyomi, Fruzsina
Vrije Universiteit Brussel
Guharoy, Mainak
Vrije Universiteit Brussel
Tompa, Peter
Vrije Universiteit Brussel
Institute of Enzymology
Data from: Functional advantages of conserved intrinsic disorder in
RNA-binding proteins
Dryad
dataset
2016
Bioinformatics
RNA-binding
2016-09-22T00:00:00Z
2016-09-22T00:00:00Z
en
https://doi.org/10.1371/journal.pone.0139731
44990327 bytes
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CC0 1.0 Universal (CC0 1.0) Public Domain Dedication
Proteins form large macromolecular assemblies with RNA that govern
essential molecular processes. RNA-binding proteins have often been
associated with conformational flexibility, yet the extent and functional
implications of their intrinsic disorder have never been fully assessed.
Here, through large-scale analysis of comprehensive protein sequence and
structure datasets we demonstrate the prevalence of intrinsic structural
disorder in RNA-binding proteins and domains. We addressed their
functionality through a quantitative description of the evolutionary
conservation of disordered segments involved in binding, and investigated
the structural implications of flexibility in terms of conformational
stability and interface formation. We conclude that the functional role of
intrinsically disordered protein segments in RNA-binding is two-fold:
first, these regions establish extended, conserved electrostatic
interfaces with RNAs via induced fit. Second, conformational flexibility
enables them to target different RNA partners, providing
multi-functionality, while also ensuring specificity. These findings
emphasize the functional importance of intrinsically disordered regions in
RNA-binding proteins.
Nucleic acid binding sequence dataThis is the sequence data in FASTA
format that underlies the analysis.sequence_data.tar.gz