ArticleJournal of biomolecular NMR2005
Structure of calmodulin complexed with an olfactory CNG channel fragment and role of the central linker: residual dipolar couplings to evaluate calmodulin binding modes outside the kinase family.
Article in Journal of biomolecular NMR, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 42 citations in OpenAlex.
- Chemical shift assignments of calmodulin bound to a C-terminal site (residues 1120-1147) in the β-subunit of a retinal cyclic nucleotide-gated channel (CNGB1).Biomolecular NMR assignments · 2022Article
- NMR Structures of Calmodulin Bound to Two Separate Regulatory Sites in the Retinal Cyclic Nucleotide-Gated Channel.Biochemistry · 2022Article
- Chemical shift assignments of calmodulin bound to the β-subunit of a retinal cyclic nucleotide-gated channel (CNGB1).Biomolecular NMR assignments · 2022Article
- Protein labeling for FRET with methoxycoumarin and acridonylalanine.Methods in enzymology · 2020Article
- Dithioamide substitutions in proteins: effects on thermostability, peptide binding, and fluorescence quenching in calmodulin.Chemical communications (Cambridge, England) · 2018Article
- A cryptophane-based "turn-on"Organic & biomolecular chemistry · 2017Article
- Multicolor protein FRET with tryptophan, selective coumarin-cysteine labeling, and genetic acridonylalanine encoding.Chemical communications (Cambridge, England) · 2017Article
- The Recognition of Calmodulin to the Target Sequence of Calcineurin-A Novel Binding Mode.Molecules (Basel, Switzerland) · 2017Article
- Efficient synthesis and in vivo incorporation of acridon-2-ylalanine, a fluorescent amino acid for lifetime and Förster resonance energy transfer/luminescence resonance energy transfer studies.Journal of the American Chemical Society · 2013Article
- Labeling proteins with fluorophore/thioamide Förster resonant energy transfer pairs by combining unnatural amino acid mutagenesis and native chemical ligation.Journal of the American Chemical Society · 2013Article
- Structural insights into neuronal K+ channel-calmodulin complexes.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Structural insights into calmodulin-regulated L-selectin ectodomain shedding.The Journal of biological chemistry · 2012Article
- Thioamide quenching of intrinsic protein fluorescence.Chemical communications (Cambridge, England) · 2012Article
- Fast methionine-based solution structure determination of calcium-calmodulin complexes.Journal of biomolecular NMR · 2011Article
- Calmodulin regulates Ca2+-sensing receptor-mediated Ca2+ signaling and its cell surface expression.The Journal of biological chemistry · 2010Article
- Analysis of protein-protein docking decoys using interaction fingerprints: application to the reconstruction of CaM-ligand complexes.BMC bioinformatics · 2010Article
- Calmodulin wraps around its binding domain in the plasma membrane Ca2+ pump anchored by a novel 18-1 motif.The Journal of biological chemistry · 2010Article
- Residual structure within the disordered C-terminal segment of p21(Waf1/Cip1/Sdi1) and its implications for molecular recognition.Protein science : a publication of the Protein Society · 2009Article
- EF-hand protein dynamics and evolution of calcium signal transduction: an NMR view.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2006Review
- Prediction of three dimensional structure of calmodulin.The protein journal · 2006Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The NMR high-resolution structure of calmodulin complexed with a fragment of the olfactory cyclic-nucleotide gated channel is described. This structure shows features that are unique for this complex, including an active role of the linker connecting the N- and C-lobes of calmodulin upon binding of the peptide. Such linker is not only involved in the formation of an hydrophobic pocket to accommodate a bulky peptide residue, but it also provides a positively charged region complementary to a negative charge of the target. This complex of calmodulin with a target not belonging to the kinase family was used to test the residual dipolar coupling (RDC) approach for the determination of calmodulin binding modes to peptides. Although the complex here characterized belongs to the (1--14) family, high Q values were obtained with all the 1:1 complexes for which crystalline structures are available. Reduction of the RDC data set used for the correlation analysis to structured regions of the complex allowed a clear identification of the binding mode. Excluded regions comprise calcium binding loops and loops connecting the EF-hand motifs.
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