Functions of short lifetime biological structures at large: the case of intrinsically disordered proteins.
By Vladimir N Uversky. 2018
24 citations recorded by the source corpus.
Although for more than a century a protein function was intimately associated with the presence of unique structure in a protein molecule, recent years witnessed a skyrocket rise of the appreciation of protein intrinsic disorder concept that emphasizes the importance of the biologically active proteins without ordered structures. In different proteins, the depth and breadth of disorder penetrance are different, generating an amusing spatiotemporal heterogeneity of intrinsically disordered proteins (IDPs) and intrinsically disordered protein region regions (IDPRs), which are typically described as highly dynamic ensembles of rapidly interconverting conformations (or a multitude of short lifetime structures). IDPs/IDPRs constitute a substantial part of protein kingdom and have unique functions complementary to functional repertoires of ordered proteins. They are recognized as interaction specialists and global controllers that play crucial roles in regulation of functions of their binding partners and in controlling large biological networks. IDPs/IDPRs are characterized by immense binding promiscuity and are able to use a broad spectrum of binding modes, often resulting in the formation of short lifetime complexes. In their turn, functions of IDPs and IDPRs are controlled by various means, such as numerous posttranslational modifications and alternative splicing. Some of the functions of IDPs/IDPRs are briefly considered in this review to shed some light on the biological roles of short-lived structures at large.
Subfields: Materials Chemistry, Molecular Biology
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Materials Chemistry
- Jack Hanson
- Kuldip K. Paliwal
- Thomas Litfin
- Yaoqi Zhou
- Jinbo Xu
- Yuedong Yang
- Sheng Wang
- Liam J. McGuffin
In Molecular Biology
- Kuldip K. Paliwal
- Jack Hanson
- Yaoqi Zhou
- Thomas Litfin
- Yuedong Yang
- Jinbo Xu
- Sheng Wang
- Jianlin Cheng
Citations in the corpus
- SPOT-Disorder2: Improved Protein Intrinsic Disorder Prediction by Ensembled Deep Learning (2019, background): “Advantaged by their disordered flexibility [4], IDPs play essential roles in signaling, assembling, and regulatory functions [5], and are implicated in numerous human diseases, such as cancer, amyloidoses, cardiovascular disease, neurodegenerative diseases, and various genetic diseases [6].”