ArticleBiophysical journal1998
Structure and dynamics of calmodulin in solution.
Article in Biophysical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 162 citations in OpenAlex.
- Let go or retain: role of calmodulin in orchestrating nuclear protein transport in eukaryotes.Plant cell reports · 2026Review
- Dynamic interactions of dimeric hub proteins underlie their diverse functions and structures: A comparative analysis of 14-3-3 and LC8.The Journal of biological chemistry · 2025Review
- Metamorphic Proteins to Achieve Conformationally Selective Material Surface Binding.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Insights of potential trypanocidal effect of the synthetic derivative (2E)-1-(4-aminophenyl)-3-(2,4-dichlorophenyl)prop-2-en-1-one: in vitro assay, MEV analysis, quantum study, molecular docking, molecular dynamics, MPO analysis, and predictive ADMET.Naunyn-Schmiedeberg's archives of pharmacology · 2024Article
- Rational Approach toward COVID-19's Main Protease Inhibitors: A Hierarchical Biochemoinformatics Analysis.International journal of molecular sciences · 2024Article
- Structures of calmodulin-melittin complexes show multiple binding modes lacking classical anchoring interactions.The Journal of biological chemistry · 2023Article
- Interdomain Dynamics via Paramagnetic NMR on the Highly Flexible Complex Calmodulin/Munc13-1.Journal of the American Chemical Society · 2022Article
- Combined Pulsed Electron Double Resonance EPR and Molecular Dynamics Investigations of Calmodulin Suggest Effects of Crowding Agents on Protein Structures.Biochemistry · 2022Article
- hdANM: a new comprehensive dynamics model for protein hinges.Biophysical journal · 2021Article
- Coarse-Grained Modeling and Molecular Dynamics Simulations of CaFrontiers in molecular biosciences · 2021Article
- Characterizing and Predicting Protein Hinges for Mechanistic Insight.Journal of molecular biology · 2020Article
- Bayesian inference of protein conformational ensembles from limited structural data.PLoS computational biology · 2018Article
- Effect of Ca2+ on the promiscuous target-protein binding of calmodulin.PLoS computational biology · 2018Article
- Article
- Discovery at the interface: Toward novel anti-proliferative agents targeting human estrogen receptor/S100 interactions.Cell cycle (Georgetown, Tex.) · 2016Article
- Computational Methods for Structural and Functional Studies of Alzheimer's Amyloid Ion Channels.Methods in molecular biology (Clifton, N.J.) · 2016Article
- Conformational frustration in calmodulin-target recognition.Journal of molecular recognition : JMR · 2015Article
- Effect of the Brugada syndrome mutation A39V on calmodulin regulation of Cav1.2 channels.Molecular brain · 2014Article
- Effect of Calcium Ion Removal, Ionic Strength, and Temperature on the Conformation Change in Calmodulin Protein at Physiological pH.Journal of biophysics (Hindawi Publishing Corporation : Online) · 2014Article
- Structural analysis of calmodulin binding to ion channels demonstrates the role of its plasticity in regulation.Pflugers Archiv : European journal of physiology · 2013Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
To characterize the dynamic behavior of calmodulin in solution, we have carried out molecular dynamics (MD) simulations of the Ca2+-loaded structure. The crystal structure of calmodulin was placed in a solvent sphere of radius 44 A, and 6 Cl- and 22 Na+ ions were included to neutralize the system and to model a 150 mM salt concentration. The total number of atoms was 32,867. During the 3-ns simulation, the structure exhibits large conformational changes on the nanosecond time scale. The central alpha-helix, which has been shown to unwind locally upon binding of calmodulin to target proteins, bends and unwinds near residue Arg74. We interpret this result as a preparative step in the more extensive structural transition observed in the "flexible linker" region 74-82 of the central helix upon complex formation. The major structural change is a reorientation of the two Ca2+-binding domains with respect to each other and a rearrangement of alpha-helices in the N-terminus domain that makes the hydrophobic target peptide binding site more accessible. This structural rearrangement brings the domains to a more favorable position for target binding, poised to achieve the orientation observed in the complex of calmodulin with myosin light-chain kinase. Analysis of solvent structure reveals an inhomogeneity in the mobility of water in the vicinity of the protein, which is attributable to the hydrophobic effect exerted by calmodulin's binding sites for target peptides.
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