Function and structure of inherently disordered proteins
Abstract
The application of bioinformatics methodologies to proteins inherently lacking 3D structure has brought increased attention to these macromolecules. Here topics concerning these proteins are discussed, including their prediction from amino acid sequence, their enrichment in eukaryotes compared to prokaryotes, their more rapid evolution compared to structured proteins, their organization into specific groups, their structural preferences, their half-lives in cells, their contributions to signaling diversity (via high contents of multiple-partner binding sites, post-translational modifications, and alternative splicing), their distinct functional repertoire compared to that of structured proteins, and their involvement in diseases.
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The combined use of intrinsic disorder, alternative splicing and PTM widely enables the context-dependent orchestration of signaling in developmental biology and other complex processes.
“The combined use of intrinsic disorder, alternative splicing and PTM widely enables the context-dependent orchestration of signaling in developmental biology and other complex processes [38, 39].”
From Intrinsically disordered proteins play diverse roles in cell signaling (2022) · cites this paper as [38]
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Keppel, T. R., Sarpong, K., Murray, E. M., Monsey, J., Zhu, J., & Bose, R. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.747485 · Cited by 29 · see citing works
- Authors
- Dunker, A. K., Silman, I., Uversky, V. N., & Sussman, J. L.
- Affiliations
- Indiana University Indianapolis (US)
- Weizmann Institute of Science (IL)
- Russian Academy of Sciences (RU)
- Corresponding author
- Sussman, Joel L
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2008-12
- Volume
- 18
- Issue
- 6
- Pages
- 756-764
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W2097891553
- Cited by
- 963
- References
- 73
- Citations by year
- 2026: 13 · 2025: 29 · 2024: 38 · 2023: 29 · 2022: 43 · 2021: 43 · 2020: 50 · 2019: 55 · 2018: 52 · 2017: 38 · 2016: 68 · 2015: 70 · 2014: 81 · 2013: 91 · 2012: 87
- FWCI
- 4.51
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Opinion in Structural Biology (publishedVersion)
- PubMed (publishedVersion)
- Digital Commons - University of South Florida (University of South Florida) (submittedVersion)
- Funders
- Autism Speaks (AS1324)
- National Institutes of Health
- Russian Academy of Sciences
- National Institute of General Medical Sciences (GM071714-01A2, R01GM071714)
- U.S. National Library of Medicine (R01LM007688)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- intrinsically disordered proteins, protein structure prediction, protein evolution, protein half-life, protein-protein interaction, post-translational modification, alternative splicing, disease association
- MeSH terms
- Animals, Disease, Humans, Protein Conformation, Proteins, Structure-Activity Relationship, Protein Folding, Evolution, Molecular, Computational Biology, Sequence Analysis, Protein
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