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Troponin calcium binding

Johnson, J.D., Collins, J.H., and Potter, J.D. (1978) Dansylaziridine labeled troponin C. A fluorescent probe of calcium ion binding to the calcium ion-specific regulatory sites./. Biol. Chem. 253, 6451. [Pg.1079]

In conclusion, troponin binds Ca2+ in six-fold coordination and all oxygen ligands are provided from amino acids. No water is needed for the coordination complex. Aspartic acid and glutamic acid occupy key positions in the four calcium binding regions of the molecule. Transfer of calcium to tropomyosin and the actin filament during contraction is achieved by coordination changes. [Pg.28]

Calcium is the trigger behind the muscle contraction process (24,25). Neural stimulation activates the release of stored Ca(Il) resulting in a dramatic increase in free calcium ion levels. The subsequent binding of Ca(Il) resulting in a dramatic increase in free calcium ion levels. The subsequent binding of Ca(Il) to the muscle protein troponin C provides the impetus for a conformational change in the troponin complex and sets off successive events resulting in muscle contraction. [Pg.409]

Table 2.2 Amino acid sequences of calcium-binding EF motifs in three different proteins Pamalbumin VKKAFAI I DQDKSGFIEEDELKLFLQNF Calmodulin FKEAFSLFDKDGDGT I TTKELGTVMRSL Troponin-C LADCFR I FDKNADGF I D lEELGE I LRAT... Table 2.2 Amino acid sequences of calcium-binding EF motifs in three different proteins Pamalbumin VKKAFAI I DQDKSGFIEEDELKLFLQNF Calmodulin FKEAFSLFDKDGDGT I TTKELGTVMRSL Troponin-C LADCFR I FDKNADGF I D lEELGE I LRAT...
Figure 6.21a) comprising two domains separated by a long straight a helix, similar in shape to troponin-C described in Chapter 2 (see Figure 2.13c). Each domain comprises two EF hands (see Figure 2.13a), each of which binds a calcium atom. The two domains are clearly separated in space at the two ends of the a helix linker. [Pg.110]

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]

Tropomyosin is thought to lie in the groove formed between the associated actin strands. The sites at which the myosin crossbridges attach are affected by the relationship between tropomyosin and the actin strands. The role of tropomyosin in smooth muscle is completely undefined while in striated muscle it is clearly involved in the activation of contraction. The difference is made clear by the absence from smooth muscle of the protein, troponin, which in striated muscle provides the binding site for the triggering calcium. [Pg.170]

In striated muscle, there are two other proteins that are minor in terms of their mass but important in terms of their function. Tropomyosin is a fibrous molecule that consists of two chains, alpha and beta, that attach to F-actin in the groove between its filaments (Figure 49-3). Tropomyosin is present in all muscular and muscle-fike structures. The troponin complex is unique to striated muscle and consists of three polypeptides. Troponin T (TpT) binds to tropomyosin as well as to the other two troponin components. Troponin I (Tpl) inhibits the F-actin-myosin interaction and also binds to the other components of troponin. Troponin C (TpC) is a calcium-binding polypeptide that is structurally and functionally analogous to calmodulin, an important calcium-binding protein widely distributed in nature. Four molecules of calcium ion are bound per molecule of troponin C or calmodulin, and both molecules have a molecular mass of 17 kDa. [Pg.562]

Site of calcium binding Troponin Calmodulin Calmodulin... [Pg.156]

Function of calcium Reposition troponin/tropomyosin to uncover myosin binding sites on actin Phosphorylate and activate myosin to bind with actin Phosphorylate and activate myosin to bind with actin... [Pg.156]

In skeletal muscle, calcium binds to troponin and causes the repositioning of tropomyosin. As a result, the myosin-binding sites on the actin become uncovered and crossbridge cycling takes place. Although an increase in cytosolic calcium is also needed in smooth muscle, its role in the mechanism of contraction is very different. Three major steps are involved in smooth muscle contraction ... [Pg.157]

Table XI (346-390) lists a number of calcium-binding proteins and indicates very succinctly their role in biological systems. This table both illustrates the range of functions of calcium-binding proteins and serves to introduce those which appear subsequently in this chapter. The structures and functions of particularly important calcium-binding proteins such as calmodulin, parvalbumin, and troponin C are described in standard texts on biochemistry. The minimal Table XI entry for the particularly important calmodulins is amplified in the next paragraph. Table XI provides a sprinkling of references to enable readers to gain entry into the literature, for these and for most of the less-familiar species. Table XI (346-390) lists a number of calcium-binding proteins and indicates very succinctly their role in biological systems. This table both illustrates the range of functions of calcium-binding proteins and serves to introduce those which appear subsequently in this chapter. The structures and functions of particularly important calcium-binding proteins such as calmodulin, parvalbumin, and troponin C are described in standard texts on biochemistry. The minimal Table XI entry for the particularly important calmodulins is amplified in the next paragraph. Table XI provides a sprinkling of references to enable readers to gain entry into the literature, for these and for most of the less-familiar species.

See other pages where Troponin calcium binding is mentioned: [Pg.144]    [Pg.194]    [Pg.301]    [Pg.302]    [Pg.221]    [Pg.314]    [Pg.58]    [Pg.75]    [Pg.93]    [Pg.758]    [Pg.314]    [Pg.20]    [Pg.130]    [Pg.865]    [Pg.36]    [Pg.945]    [Pg.839]    [Pg.454]    [Pg.60]    [Pg.1027]    [Pg.127]    [Pg.1010]    [Pg.127]    [Pg.25]    [Pg.26]    [Pg.546]    [Pg.24]    [Pg.67]    [Pg.67]    [Pg.173]    [Pg.463]    [Pg.143]    [Pg.152]    [Pg.258]    [Pg.261]    [Pg.293]   
See also in sourсe #XX -- [ Pg.180 ]




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