ArticleProteins2011
Recognition of β-calcineurin by the domains of calmodulin: thermodynamic and structural evidence for distinct roles.
Article in Proteins, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 35 citations in OpenAlex.
- NaStructure (London, England : 1993) · 2021Article
- Assessing the Role of Calmodulin's Linker Flexibility in Target Binding.International journal of molecular sciences · 2021Article
- Calcineurin.Cell communication and signaling : CCS · 2020Review
- Neurogranin stimulates Ca2+/calmodulin-dependent kinase II by suppressing calcineurin activity at specific calcium spike frequencies.PLoS computational biology · 2020Article
- Uncertainty quantification, propagation and characterization by Bayesian analysis combined with global sensitivity analysis applied to dynamical intracellular pathway models.Bioinformatics (Oxford, England) · 2019Article
- Backbone and side-chain resonance assignments of (CaBiomolecular NMR assignments · 2017Article
- The Recognition of Calmodulin to the Target Sequence of Calcineurin-A Novel Binding Mode.Molecules (Basel, Switzerland) · 2017Article
- Calcium triggers reversal of calmodulin on nested anti-parallel sites in the IQ motif of the neuronal voltage-dependent sodium channel NaBiophysical chemistry · 2017Article
- Opposing Intermolecular Tuning of CaBiophysical journal · 2017Article
- Calcineurin in a Crowded World.Biochemistry · 2016Article
- Modelling intracellular competition for calcium: kinetic and thermodynamic control of different molecular modes of signal decoding.Scientific reports · 2016Article
- Modulation of calmodulin lobes by different targets: an allosteric model with hemiconcerted conformational transitions.PLoS computational biology · 2015Article
- Mechanisms of regulation of olfactory transduction and adaptation in the olfactory cilium.PloS one · 2014Article
- Modeling intracellular signaling underlying striatal function in health and disease.Progress in molecular biology and translational science · 2014Review
- A calcineurin docking motif (LXVP) in dynamin-related protein 1 contributes to mitochondrial fragmentation and ischemic neuronal injury.The Journal of biological chemistry · 2013Article
- Structural basis for activation of calcineurin by calmodulin.Journal of molecular biology · 2012Article
- Article
- Thermodynamic linkage between calmodulin domains binding calcium and contiguous sites in the C-terminal tail of Ca(V)1.2.Biophysical chemistry · 2011Article
- Transient disorder: Calcineurin as an example.Intrinsically disordered proteinsReview
- Calcium-dependent energetics of calmodulin domain interactions with regulatory regions of the Ryanodine Receptor Type 1 (RyR1).Biophysical chemistryArticle
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4 authors at 1 institution in 1 country.
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Abstract
Calcineurin (CaN, PP2B, PPP3), a heterodimeric Ca(2+)-calmodulin-dependent Ser/Thr phosphatase, regulates swimming in Paramecia, stress responses in yeast, and T-cell activation and cardiac hypertrophy in humans. Calcium binding to CaN(B) (the regulatory subunit) triggers conformational change in CaN(A) (the catalytic subunit). Two isoforms of CaN(A) (α, β) are both abundant in brain and heart and activated by calcium-saturated calmodulin (CaM). The individual contribution of each domain of CaM to regulation of calcineurin is not known. Hydrodynamic analyses of (Ca(2+))₄-CaM(1-148) bound to βCaNp, a peptide representing its CaM-binding domain, indicated a 1:1 stoichiometry. βCaNp binding to CaM increased the affinity of calcium for the N- and C-domains equally, thus preserving intrinsic domain differences, and the preference of calcium for sites III and IV. The equilibrium constants for individual calcium-saturated CaM domains dissociating from βCaNp were ∼1 μM. A limiting K(d) ≤ 1 nM was measured directly for full-length CaM, while thermodynamic linkage analysis indicated that it was approximately 1 pM. βCaNp binding to ¹⁵N-(Ca(2+))₄-CaM(1-148) monitored by ¹⁵N/¹HN HSQC NMR showed that association perturbed the N-domain of CaM more than its C-domain. NMR resonance assignments of CaM and βCaNp, and interpretation of intermolecular NOEs observed in the ¹³C-edited and ¹²C-¹⁴N-filtered 3D NOESY spectrum indicated anti-parallel binding. The sole aromatic residue (Phe) located near the βCaNp C-terminus was in close contact with several residues of the N-domain of CaM outside the hydrophobic cleft. These structural and thermodynamic properties would permit the domains of CaM to have distinct physiological roles in regulating activation of βCaN.
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