Binding of intrinsically disordered proteins is not necessarily accompanied by a structural transition to a folded form
Open accessAbstract
There are a large number of protein domains and even entire proteins, lacking ordered structure under physiological conditions. Intriguingly, a highly flexible, random coil-like conformation is the native and functional state for many proteins known to be involved in cell signaling. An example is a key component of immune signaling, the cytoplasmic region of the T cell receptor zeta subunit. This domain exhibits specific dimerization that is distinct from non-specific aggregation behavior seen in many systems. In this work, we use diffusion and chemical shift mapping NMR data to show that the protein does not undergo a transition between disordered and ordered states upon dimerization. This finding opposes the generally accepted view on the behavior of intrinsically disordered proteins, provides evidence for the existence of specific dimerization interactions for intrinsically disordered protein species and opens a new line of research in this new and quickly developing field.
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Some IDPs/IDRs may remain unfolded and dynamic even in the bound state, creating fuzzy complexes.
“Some IDPs/IDRs may remain unfolded and dynamic even in the bound state [19–23], creating fuzzy complexes (Fig. 1) [24, 25].”
From Intrinsically disordered proteins play diverse roles in cell signaling (2022) · cites this paper as [22]
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Intrinsically disordered proteins play diverse roles in cell signaling
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Self-citation
- Authors
- Sigalov, A. B., Zhuravleva, A. V., & Orekhov, V. Y.
- Affiliations
- University of Massachusetts Chan Medical School (US)
- University of Gothenburg (SE)
- Corresponding author
- Sigalov, Alexander B.
- Venue
- Biochimie
- Publisher
- Elsevier BV
- Published
- 2007-03
- Volume
- 89
- Issue
- 3
- Pages
- 419-421
- ISSN
- 0037-9042 (ISSN-L)
- 0300-9084
- PMC
- PMC2692994
- OpenAlex
- W2021172121
- Cited by
- 128
- References
- 12
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 7 · 2023: 3 · 2022: 6 · 2021: 6 · 2020: 7 · 2019: 10 · 2018: 7 · 2017: 6 · 2016: 7 · 2015: 3 · 2014: 6 · 2013: 12 · 2012: 5
- FWCI
- 2.44
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biochimie (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (P30 AI42845-08, P30AI042845)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Chemistry › Spectroscopy › Advanced NMR Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- intrinsically disordered proteins, protein dimerization, random coil, protein-protein binding, conformational change, immune signaling, diffusion NMR, chemical shift mapping
- MeSH terms
- Protein Binding, Proteins, Protein Structure, Tertiary, Protein Folding, Dimerization, Nuclear Magnetic Resonance, Biomolecular
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