ArticleProtein science : a publication of the Protein Society2000
Enhancement by Mg2+ of domain specificity in Ca2+-dependent interactions of calmodulin with target sequences.
Article in Protein science : a publication of the Protein Society, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 49 citations in OpenAlex.
- Molecular basis for a CaThe Journal of biological chemistry · 2026Article
- Mrs2-mediated mitochondrial magnesium uptake is essential for the regulation of MCU-mediated mitochondrial CaMitochondrion · 2024Article
- Physiology of intracellular calcium buffering.Physiological reviews · 2023Review
- Physiologically Relevant Free CaJournal of molecular biology · 2021Article
- Magnesium Deficiency Causes a Reversible, Metabolic, Diastolic Cardiomyopathy.Journal of the American Heart Association · 2021Article
- Magnesium, Oxidative Stress, Inflammation, and Cardiovascular Disease.Antioxidants (Basel, Switzerland) · 2020Review
- Mechanism of β-actin mRNA Recognition by ZBP1.Cell reports · 2017Article
- The Involvement of MgOxidative medicine and cellular longevity · 2017Review
- Modulation of calmodulin lobes by different targets: an allosteric model with hemiconcerted conformational transitions.PLoS computational biology · 2015Article
- Calmodulin transduces Ca2+ oscillations into differential regulation of its target proteins.ACS chemical neuroscience · 2013Article
- Noncanonical G recognition mediates KSRP regulation of let-7 biogenesis.Nature structural & molecular biology · 2012Article
- Article
- Insights into modulation of calcium signaling by magnesium in calmodulin, troponin C and related EF-hand proteins.Biochimica et biophysica acta · 2011Review
- Solution structure and fluctuation of the Mg(2+)-bound form of calmodulin C-terminal domain.Protein science : a publication of the Protein Society · 2011Article
- Virus assembly occurs following a pH- or Ca2+-triggered switch in the thermodynamic attraction between structural protein capsomeres.Journal of the Royal Society, Interface · 2010Article
- The solution structure of the Mg2+ form of soybean calmodulin isoform 4 reveals unique features of plant calmodulins in resting cells.Protein science : a publication of the Protein Society · 2010Article
- Osmolyte-induced perturbations of hydrogen bonding between hydration layer waters: correlation with protein conformational changes.The journal of physical chemistry. B · 2009Article
- Electrospray ionization mass spectrometry studies of noncovalent myosin VI complexes reveal a new specific calmodulin binding site.Journal of the American Society for Mass Spectrometry · 2005Article
- The role of electrostatic interactions in calmodulin-peptide complex formation.Biophysical journal · 2004Article
- Relative affinity constants by electrospray ionization and Fourier transform ion cyclotron resonance mass spectrometry: calmodulin binding to peptide analogs of myosin light chain kinase.Biophysical journal · 2003Article
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3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mg2+ binds to calmodulin without inducing the changes in secondary structure that are characteristic of Ca2+ binding, or the exposure of hydrophobic surfaces that are involved in typical Ca2+-dependent target interactions. The binding of Mg2+ does, however, produce significant spectroscopic changes in residues located in the Ca2+-binding loops, and the Mg-calmodulin complex is significantly different from apo-calmodulin in loop conformation. Direct measurement of Mg2+ binding constants, and the effects of Mg2+ on Ca2+ binding to calmodulin, are consistent with specific binding of Mg2+, in competition with Ca2+. Mg2+ increases the thermodynamic stability of calmodulin, and we conclude that under resting, nonstimulated conditions, cellular Mg2+ has a direct role in conferring stability on both domains of apo-calmodulin. Apo-calmodulin binds typical target sequences from skeletal muscle myosin light chain kinase and neuromodulin with Kd approximately 70-90 nM (at low ionic strength). These affinities are virtually unchanged by 5 mM Mg2+, in marked contrast to the strong enhancement of peptide affinity induced by Ca2+. Under conditions of stimulation and increased [Ca2+], Mg2+ has a role in directing the mode of initial target binding preferentially to the C-domain of calmodulin, due to the opposite relative affinities for binding of Ca2+ and Mg2+ to the two domains. Mg2+ thus amplifies the intrinsic differences of the domains, in a target specific manner. It also contributes to setting the Ca2+ threshold for enzyme activation and increases the importance of a partially Ca2+-saturated calmodulin-target complex that can act as a regulatory kinetic and equilibrium intermediate in Ca2+-dependent target interactions.
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