ReviewJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2006
EF-hand protein dynamics and evolution of calcium signal transduction: an NMR view.
Review in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 62 citations in OpenAlex.
- DNA origami-enhanced force spectroscopy and AlphaFold structural analyses reveal the folding landscape of calcium-binding proteins.Science advances · 2025Article
- Investigation of Mutated in Colorectal Cancer (MCC) Gene Family Evolution History Indicates a Putative Role in Th17/Treg Differentiation.International journal of molecular sciences · 2023Article
- Comparative Genomics Reveals 13 Different Isoforms of Mytimycins (A-M) inInternational journal of molecular sciences · 2021Article
- Coarse-Grained Modeling and Molecular Dynamics Simulations of CaFrontiers in molecular biosciences · 2021Article
- Conformational dynamics of Ca2+-dependent responses in the polycystin-2 C-terminal tail.The Biochemical journal · 2016Article
- Oligomerization of the polycystin-2 C-terminal tail and effects on its Ca2+-binding properties.The Journal of biological chemistry · 2015Article
- In silico assessment of S100A12 monomer and dimer structural dynamics: implications for the understanding of its metal-induced conformational changes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- The number and location of EF hand motifs dictates the calcium dependence of polycystin-2 function.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014Article
- Thermodynamics and molecular dynamics simulations of calcium binding to the regulatory site of human cardiac troponin C: evidence for communication with the structural calcium binding sites.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013Article
- Cloning and characterization of a calcium binding EF-hand protein gene TaCab1 from wheat and its expression in response to Puccinia striiformis f. sp. tritici and abiotic stresses.Molecular biology reports · 2011Article
- N-terminal myristoylation alters the calcium binding pathways in neuronal calcium sensor-1.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011Article
- Electron-nuclear interactions as probes of domain motion in proteins.The Journal of chemical physics · 2010Article
- Structural characterization of a novel Ca2+-binding protein from Entamoeba histolytica: structural basis for the observed functional differences with its isoform.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2009Article
- Dynamics and energetics: a consensus analysis of the impact of calcium on EF-CaM protein complex.Biophysical journal · 2009Article
- Activation of the SK potassium channel-calmodulin complex by nanomolar concentrations of terbium.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Structure and dynamics of Ca2+-binding domain 1 of the Na+/Ca2+ exchanger in the presence and in the absence of Ca2+.Journal of molecular biology · 2008Article
- Rational design of a novel calcium-binding site adjacent to the ligand-binding site on CD2 increases its CD48 affinity.Protein science : a publication of the Protein Society · 2008Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Calcium signaling, one of the most widespread signaling mechanisms in cells, is generally carried out by EF-hand proteins, characterized by a helix-loop-helix motif paired in functional domains. EF-hand proteins may be viewed as molecular switches activated by calcium concentration transients. The EF-hand structural database has grown to a point where meaningful inferences on the functional conformational rearrangements upon calcium binding can be made by comparing a fair number of pairs of end points, i.e., the structures of the apo and calcium-bound forms. More compact descriptors of the movement associated with calcium binding, in terms of principal component analysis of the six interhelical angles, have also become available. Dynamic information obtained by NMR, also with the aid of calcium substitution with paramagnetic lanthanides, is shedding light on the intrinsic amplitude of the conformational degrees of freedom sampled by the various members of the EF-hand superfamily, as well as on the time scales of the motions. Particularly, NMR of lanthanide derivatives helps in capturing long time scale motions. Both static and dynamic pictures reveal a large variety of behaviors. It is increasingly recognized that the EF-hand machinery has differentiated its behavior during evolution in several ways, e.g., by modifying one of the loops, by undergoing a further duplication after the initial motif duplication that originated the functional domain, or by acquiring the ability to dimerize.
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