Attributes of short linear motifs
European Molecular Biology Laboratory · European Molecular Biology Laboratory · +1 more institution
Abstract
Traditionally, protein-protein interactions were thought to be mediated by large, structured domains. However, it has become clear that the interactome comprises a wide range of binding interfaces with varying degrees of flexibility, ranging from rigid globular domains to disordered regions that natively lack structure. Enrichment for disorder in highly connected hub proteins and its correlation with organism complexity hint at the functional importance of disordered regions. Nevertheless, they have not yet been extensively characterised. Shifting the attention from globular domains to disordered regions of the proteome might bring us closer to elucidating the dense and complex connectivity of the interactome.…
Citation impact
- FWCI
- 15.03
- Percentile
- 100%
- References
- 105
Authors
10- NENorman E. DaveyCorresponding
European Molecular Biology Laboratory, European Molecular Biology Laboratory
- KVKim Van Roey
European Molecular Biology Laboratory, European Molecular Biology Laboratory
- RJRobert J. Weatheritt
European Molecular Biology Laboratory, European Molecular Biology Laboratory
- GTGrischa Toedt
European Molecular Biology Laboratory, European Molecular Biology Laboratory
- BUBora Uyar
European Molecular Biology Laboratory, European Molecular Biology Laboratory
Topics & keywords
- Interactome
- Computational biology
- Proteome
- Intrinsically disordered proteins
- Biology
- Globular protein
- Structural motif
- Flexibility (engineering)