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Structural basis of calcineurin activation by calmodulin.

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Calcineurin is the only known calmodulin (CaM) activated protein phosphatase, which is involved in the regulation of numerous cellular and developmental processes and in calcium-dependent signal transduction. Although commonly assumed that CaM displaces the autoinhibitory domain (AID) blocking

Regulation of preimplantation development of mouse embryos: effects of inhibition of myosin light-chain kinase, a Ca2+/calmodulin-dependent enzyme.

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We have examined the effects of ML-9 and wortmannin, which are, respectively, specific reversible and irreversible inhibitors of myosin light-chain kinase, a Ca2+/calmodulin-dependent enzyme, on preimplantation development of the mouse in an attempt to establish a regulatory role for this enzyme in

The N-terminal domain of MDM2 resembles calmodulin and its relatives.

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It is shown here that the N-terminal domain of MDM2, which is not thought to bind calcium ions, otherwise bears a striking resemblance to a cluster of four EF-hand modules like those found in the calmodulin family. There are similarities in module arrangement, supersecondary structure and the

Toward a model of the calmodulin-myosin light-chain kinase complex: implications for calmodulin function.

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We have developed a model for the interaction of calmodulin and the presumptive calmodulin binding domain of rabbit skeletal muscle myosin light-chain kinase. In our model there is a bend in the central helix of calmodulin such that hydrophobic patches associated with the pairs of Ca2+ binding

Gain-of-function mutations in a human calmodulin-like protein identify residues critical for calmodulin action in yeast.

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A human epithelial cell-specific transcript (NB-1) encodes a calmodulin-like protein (hCLP), which is identical in length and 85% identical in amino acid sequence to authentic human calmodulin (hCaM). Although hCaM shares only 60% amino acid sequence identity with yeast calmodulin (CMD1 gene

The effect of calmodulin antagonist berbaminederivative-EBB on hepatoma in vitro and in vivo.

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OBJECTIVE To evaluate the anti-hepatoma effect of Calmodulin antagonist 0 - 4-ethoxyl-butyl-Berbamine (EBB), one of the berbamine derivatives. METHODS Monotetrazolium (MTT) method was used to analyze the effect of EBB on the proliferation and growth inhibition effect. Of a hepatoma cell line in

Kinase recognition by calmodulin: modeling the interaction with the autoinhibitory region of human cardiac titin kinase.

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Calmodulin (CaM)-protein interactions are usually described by studying complexes between synthetic targets of ca 25 amino acids and CaM. To understand the relevance of contacts outside the protein-binding region, we investigated the complex between recombinant human CaM (hCaM) and P7, a 38-residue

Differential profiles of salivary proteins with affinity to Streptococcus mutans lipoteichoic acid in caries-free and caries-positive human subjects.

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Streptococcus mutans is a representative oral pathogen that causes dental caries and pulpal inflammation. Its lipoteichoic acid (Sm.LTA) is known to be an important cell-wall virulence factor involved in bacterial adhesion and induction of inflammation. Since Sm.LTA-binding proteins (Sm.LTA-BPs)

Chemiluminescence response of beta-glucan stimulated leukocytes isolated from different tissues and peritoneal cavity of Dicentrarchus labrax.

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The respiratory burst of leukocytes isolated from sea bass (Dicentrarchus labrax) pronephros, peritoneal cavity (P.C.), spleen and blood, was measured by a chemiluminescence (CL) assay after stimulation with beta-glucan. The CL response by P.C. and pronephros leukocytes was significantly higher than

Ionic interactions are essential for TRPV1 C-terminus binding to calmodulin.

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Calmodulin (CaM) is known to play an important role in the regulation of TRP channels activity. Although it has been reported that CaM binds to the C-terminus of TRPV1 (TRPV1-CT), no classic CaM-binding motif was found in this region. In this work, we explored this unusual TRPV1 CaM-binding motif in

Calmodulin in Paramecium tetraurelia: localization from the in vivo to the ultrastructural level.

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Monospecific polyclonal antibodies against Paramecium tetraurelia calmodulin were prepared and labeled for calmodulin localization on different levels of resolution: by microinjection into living cells; with isolated cell surface complexes (cortices); on the ultrastructural level, using Lowicryl

Effect of tacrine on cytosolic Ca2+ level and calmodulin in gastric muscle tissues of rat.

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BACKGROUND Tacrine is an acetylcholinesterase inhibitor. It has an indirect cholinomimetic effect inducing contractions of the gastric smooth muscles. The contractions are related to the effect of the accumulated acetylcholine in tissues on the respective choline receptors. There is a well defined

Structural Basis for the Recognition of Eukaryotic Elongation Factor 2 Kinase by Calmodulin.

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Binding of Ca(2+)-loaded calmodulin (CaM) activates eukaryotic elongation factor 2 kinase (eEF-2K) that phosphorylates eEF-2, its only known cellular target, leading to a decrease in global protein synthesis. Here, using an eEF-2K-derived peptide (eEF-2KCBD) that encodes the region necessary for its

Calmodulin binding to alpha 1-purothionin: solution binding and modeling of the complex.

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CD and fluorescence spectroscopic measurements show that calmodulin (CaM) binds to purothionins (alpha 1-purothionin: alpha 1-PT; beta-purothionin: beta-PT) in 1:1 stoichiometry with an affinity similar to that exhibited with the tightest binding CaM-binding peptides. Using the available crystal

High throughput screening, docking, and molecular dynamics studies to identify potential inhibitors of human calcium/calmodulin-dependent protein kinase IV.

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Calcium/calmodulin-dependent protein kinase IV (CAMKIV) is associated with many diseases including cancer and neurodegenerative disorders and thus being considered as a potential drug target. Here, we have employed the knowledge of three-dimensional structure of CAMKIV to identify new inhibitors for

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