ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2015
Thermodynamics of Calcium binding to the Calmodulin N-terminal domain to evaluate site-specific affinity constants and cooperativity.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed.
- Calcium dissociation with carbonate ions from Pf-SCP, sarcoplasmic calcium-binding protein in Pinctada fucata, contributes to calcium mineralization for shell formation.Protein science : a publication of the Protein Society · 2025Article
- Thermodynamics of calcium binding to heparin: Implications of solvation and water structuring for polysaccharide biofunctions.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Calcium mediated static and dynamic allostery in S100A12: Implications for target recognition by S100 proteins.Protein science : a publication of the Protein Society · 2024Article
- Article
- Inter-Site Cooperativity of Calmodulin N-Terminal Domain and Phosphorylation Synergistically Improve the Affinity and Selectivity for Uranyl.Biomolecules · 2022Article
- Phosphorylation promotes the endonuclease-like activity of human centrin 2.RSC advances · 2022Article
- Study on the interaction ofRSC advances · 2021Article
- Solution NMR Structure of Titin N2A Region Ig Domain I83 and Its Interaction with Metal Ions.Journal of molecular biology · 2021Article
- The mechanism of complex formation between calmodulin and voltage gated calcium channels revealed by molecular dynamics.PloS one · 2021Article
- Quantitative Determination of CaBio-protocol · 2020Article
- CaFrontiers in plant science · 2020Review
- Calcium binding to a disordered domain of a type III-secreted protein from a coral pathogen promotes secondary structure formation and catalytic activity.Scientific reports · 2019Article
- Crystal structure of the trimeric N-terminal domain of ciliate Euplotes octocarinatus centrin binding with calcium ions.Protein science : a publication of the Protein Society · 2018Article
- Calmodulinopathy: A Novel, Life-Threatening Clinical Entity Affecting the Young.Frontiers in cardiovascular medicine · 2018Review
- Conserved properties of individual Ca2+-binding sites in calmodulin.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
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8 authors.
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Abstract
Calmodulin (CaM) is an essential Ca(II)-dependent regulator of cell physiology. To understand its interaction with Ca(II) at a molecular level, it is essential to examine Ca(II) binding at each site of the protein, even if it is challenging to estimate the site-specific binding properties of the interdependent CaM-binding sites. In this study, we evaluated the site-specific Ca(II)-binding affinity of sites I and II of the N-terminal domain by combining site-directed mutagenesis and spectrofluorimetry. The mutations had very low impact on the protein structure and stability. We used these binding constants to evaluate the inter-site cooperativity energy and compared it with its lower limit value usually reported in the literature. We found that site I affinity for Ca(II) was 1.5 times that of site II and that cooperativity induced an approximately tenfold higher affinity for the second Ca(II)-binding event, as compared to the first one. We further showed that insertion of a tryptophan at position 7 of site II binding loop significantly increased site II affinity for Ca(II) and the intra-domain cooperativity. ΔH and ΔS parameters were studied by isothermal titration calorimetry for Ca(II) binding to site I, site II and to the entire N-terminal domain. They showed that calcium binding is mainly entropy driven for the first and second binding events. These findings provide molecular information on the structure-affinity relationship of the individual sites of the CaM N-terminal domain and new perspectives for the optimization of metal ion binding by mutating the EF-hand loops sequences.
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