Natively unfolded C‐terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin
Abstract
The structure of C‐terminal domain (CaD136, C‐terminal residues 636–771) of chicken gizzard caldesmon has been analyzed by a variety of physico‐chemical methods. We are showing here that CaD136 does not have globular structure, has low secondary structure content, is essentially noncompact, as it follows from high Rg and RS values, and is characterized by the absence of distinct heat absorption peaks, i.e. it belongs to the family of natively unfolded (or intrinsically unstructured) proteins. Surprisingly, effective binding of single calmodulin molecule (Kd = 1.4 ± 0.2 μM) leads only to a very moderate folding of this protein and CaD136 remains substantially unfolded within its tight complex with calmodulin. The biological significance of these observations is discussed. Proteins 2003. © 2003 Wiley‐Liss, Inc.
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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 [21]
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Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling
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- Authors
- Permyakov, S. E., Millett, I. S., Doniach, S., Permyakov, E. A., & Uversky, V. N.
- Affiliations
- Russian Academy of Sciences (RU)
- Stanford University (US)
- Corresponding author
- Uversky, Vladimir N.
- Venue
- Proteins: Structure, Function, and Bioinformatics
- Publisher
- Wiley
- Published
- 2003-10-22
- Volume
- 53
- Issue
- 4
- Pages
- 855
- ISSN
- 0887-3585 (ISSN-L)
- 1097-0134
- OpenAlex
- W2076772188
- Cited by
- 113
- References
- 53
- Citations by year
- 2025: 4 · 2024: 7 · 2023: 4 · 2022: 9 · 2021: 2 · 2020: 8 · 2019: 4 · 2018: 1 · 2017: 6 · 2016: 6 · 2015: 9 · 2014: 3 · 2013: 5 · 2012: 6
- FWCI
- 1.15
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Proteins Structure Function and Bioinformatics (publishedVersion)
- PubMed (publishedVersion)
- Digital Commons - University of South Florida (University of South Florida) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- caldesmon, calmodulin, intrinsically disordered proteins, protein-protein binding, protein folding, C-terminal domain, chicken gizzard, radius of gyration, secondary structure content, heat absorption
- MeSH terms
- Amino Acids, Animals, Calmodulin, Calmodulin-Binding Proteins, Chickens, Circular Dichroism, Protein Binding, Spectrometry, Fluorescence, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Folding, Hydrophobic and Hydrophilic Interactions
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