Cited by 113Protein Structure and DynamicsProtein Interaction Studies and Fluorescence AnalysisHeat shock proteins research

Natively unfolded C‐terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin

Permyakov, Sergei E., Millett, Ian S., Doniach, Sebastian, Permyakov, Eugene A., Uversky, Vladimir N.·2003·Proteins: Structure, Function, and Bioinformatics

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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Crossref · 10.1002/prot.10481

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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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