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Calmodulin sites

A human gene for hepatic inducible NOS was isolated in 1993 by Geller and coworkers76. Hepatocytes were isolated from an operative wedge resection, which were over 98% pure. The cells were stimulated with cytokines TNF-a, IL-1 and IFN-y. The purified cDNA, in addition to FMN, FAD and NADPH factors, also contained a calmodulin site. This site retained some activity in the presence of calcium inhibitors. There are also phosphorylation sites at 232, 576 and 890 residues. [Pg.979]

FIGURES Amodelof the two-dimensional structure of domain 4 derived from structural and functional studies. This hypothetical structure shows domain 4 of CD bound to Ca +calmodulin. Sites A,B, and B are indicated as including both lobes of calmodulin bound in an extended conformation, together with CD tryptophans 716,749, and 779. The peptide chain is looped so that the three tryptophans and tyrosine 682 and histidine 667 are within 1.5 nm of cysteine 636. The exons are indicated by alternating shading of the peptide chain. Exon 11 is the loop at the bottom, which includes tryptophan 749 and the MAP kinase site serine 759. [Pg.83]

Although intended for the biochemistry lab, this experiment provides analytical students with a practical characterization analysis. Of particular interest is the use of Job s method to determine the number of TNS (2-p-toludinylnaphthalene-6-sulfonate) binding sites on calmodulin, fluorescence is measured at 475 nm using an excitation wavelength of 330 nm. [Pg.449]

Nonrepetitive but well-defined structures of this type form many important features of enzyme active sites. In some cases, a particular arrangement of coil structure providing a specific type of functional site recurs in several functionally related proteins. The peptide loop that binds iron-sulfur clusters in both ferredoxin and high potential iron protein is one example. Another is the central loop portion of the E—F hand structure that binds a calcium ion in several calcium-binding proteins, including calmodulin, carp parvalbumin, troponin C, and the intestinal calcium-binding protein. This loop, shown in Figure 6.26, connects two short a-helices. The calcium ion nestles into the pocket formed by this structure. [Pg.182]

TPR) domains. PP2B (calcineurin) is a heterodimer of a catalytic A-subunit together with a regulatory, Ca2+-binding B-subunit. The A-subunit additionally carries a calmodulin binding site and an autoinhibitory domain. PP7 also contains EF-hand motifs. Both, PP2B and PP7 are stimulated by Ca2+-ions. [Pg.1013]

Other studies have demonstrated that the skeletal muscle ai peptide can be phosphorylated in T-tubule membranes by a multifunctional Ca " /calmodulin (CaM)-dependent protein kinase [111], Phosphorylation occurs on the i subunit to an extent of 2 mol phosphate/mol subunit and on the /i subunit to an extent of 0.7-1 mol phosphate/mol channel [108,111]. Phosphorylation catalyzed by the CaM-kinase on the ai subunit is additive to that caused by PKA and occurs on distinct sites [111]. So far, however, we have not observed any functional consequences of phosphorylation of the skeletal muscle Ca channels by the CaM-kinase. [Pg.330]

Fig. 13. The binding sites of calcium in (a) parvalbumin (41a), (b) annexin (41) and (c) calmodulin (42). The drawings show two bidentate carboxylates coordinated to Ca2 in the EF-hand site of parvalbumin, and one bidentate carboxylate coordinated to Ca2 in annexin and calmodulin. All the donor atoms coordinated to the calciums are oxygen donor atoms from carboxylates of asp = aspartate, or glu = glutamate, or else peptide carbonyl oxygens from gly = glycine or met = methionine. Redrawn after Refs. (41-42). Fig. 13. The binding sites of calcium in (a) parvalbumin (41a), (b) annexin (41) and (c) calmodulin (42). The drawings show two bidentate carboxylates coordinated to Ca2 in the EF-hand site of parvalbumin, and one bidentate carboxylate coordinated to Ca2 in annexin and calmodulin. All the donor atoms coordinated to the calciums are oxygen donor atoms from carboxylates of asp = aspartate, or glu = glutamate, or else peptide carbonyl oxygens from gly = glycine or met = methionine. Redrawn after Refs. (41-42).
Site of calcium binding Troponin Calmodulin Calmodulin... [Pg.156]

Schepartz, A., and Cuenoud, B. (1990) Site-specific cleavage of the protein calmodulin using a trifluoperazine-based affinity reagent./. Am. Chem. Soc. 112, 3247-3249. [Pg.1111]

Schmidt, A., Kalkhof, S., Ihling, C., Schulz, D.M., Beck-Sickinger, A.G., Cooper, D.M.E, and Sinz, A. (2005) Studying calmodulin/adenylyl cyclase 8 interaction using isotope-labeled cross-linkers and FTICR mass spectrometry. Poster, Pierce Biotechnology web site. [Pg.1111]


See other pages where Calmodulin sites is mentioned: [Pg.977]    [Pg.989]    [Pg.309]    [Pg.321]    [Pg.136]    [Pg.977]    [Pg.989]    [Pg.309]    [Pg.321]    [Pg.136]    [Pg.211]    [Pg.543]    [Pg.29]    [Pg.32]    [Pg.33]    [Pg.664]    [Pg.810]    [Pg.857]    [Pg.862]    [Pg.863]    [Pg.865]    [Pg.963]    [Pg.1308]    [Pg.68]    [Pg.173]    [Pg.174]    [Pg.174]    [Pg.175]    [Pg.177]    [Pg.14]    [Pg.148]    [Pg.463]    [Pg.465]    [Pg.95]    [Pg.238]    [Pg.62]    [Pg.69]    [Pg.70]    [Pg.263]    [Pg.116]    [Pg.260]    [Pg.298]    [Pg.158]    [Pg.1032]   
See also in sourсe #XX -- [ Pg.133 ]




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