ArticleScientific reports2019
Molecular Dynamics Study of the Changes in Conformation of Calmodulin with Calcium Binding and/or Target Recognition.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- ConforFold recovers alternative protein conformations beyond MSA subsampling.Protein science : a publication of the Protein Society · 2026Article
- Improving the Thermostability of the Qβ Bacteriophage Coat Protein Through Single-Site Mutation Based on Molecular Dynamics.International journal of molecular sciences · 2026Article
- Theoretical evaluation of the biological activity of hydrogen.Medical gas research · 2025Review
- Structure-based virtual screening against multiple Plasmodium falciparum kinases reveals antimalarial compounds.Molecular diversity · 2024Article
- Probing calmodulin-NO synthase interactions via site-specific infrared spectroscopy: an introductory investigation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Article
- Design of hACE2-based small peptide inhibitors against spike protein of SARS-CoV-2: a computational approach.Structural chemistry · 2023Article
- Crosstalk among Calcium ATPases: PMCA, SERCA and SPCA in Mental Diseases.International journal of molecular sciences · 2021Review
- The mechanism of complex formation between calmodulin and voltage gated calcium channels revealed by molecular dynamics.PloS one · 2021Article
- Influence of Calcium Binding on Conformations and Motions of Anionic Polyamino Acids. Effect of Side Chain Length.Polymers · 2020Article
- Structural dynamic studies on identification of EGCG analogues for the inhibition of Human Papillomavirus E7.Scientific reports · 2020Article
- CaThe Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2020Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Calmodulin is a calcium binding protein with two lobes, N-lobe and C-lobe, which evolved from duplication and fusion of a single precursor lobe of a pair of EF-hand. These two lobes of calmodulin show subtle differences in calcium binding and target recognition; these are important for the functions of calmodulin. Since the structures, especially main chain conformations, of two EF-lobes in holo-form are quite similar; this is a good example to evaluate the effect of side chains for structural dynamics. We analyzed the structure of calmodulin using molecular dynamics and found differences in conformational ensembles between N- and C-lobes. We also showed the mutant structures created by homology modeling could reproduce the difference of dynamic motion between N- and C-lobes.
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