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Light-chain binding domain

Warshaw, D. M., Guilford, W. H., Freyzon, Y., Krementsova, E., Palmiter, K. A., Tyska, M. J., Baker, J. E., and Trybus, K. M. (2000). The light chain binding domain of expressed smooth muscle heavy meromyosin acts as a mechanical lever./. Biol. Chem. 275, 37167-37172. [Pg.194]

Kinesin-1 comprises three major domains the N-terminal motor domain that can be subdivided into the core motor domain and the adjacent neck linker and neck region, the central stalk domain, and the C-terminal tail or light chain-binding domain (Fig. 1A). The core motor domain has a length of about 325 amino acids and contains both the microtubule and the nucleotide binding elements. In different kinesin families, this motor... [Pg.300]

Kastem W, Sjobring U, Bjorck L Structure of peptostreptococcal protein L and identification of a repeated immunoglobulin light chain-binding domain. J Biol Chem 1992 267 12820-12825. [Pg.212]

Humans have five classes of immunoglobulins, each with different biological functions. The most abundant class is IgG, a Y-shaped protein with two heavy and two light chains. The domains near the upper ends of the Y are hypervariable within the broad population of IgGs and form two antigen-binding sites. [Pg.182]

Nilson, B. H., Logdberg, L., Kastern, W., Bjorck, L., and Akerstrom, B. (1993). Purification of antibodies using protein L-binding framework structures in the light chain variable domain. J. Immunol. Methods 164, 33-40. [Pg.628]

The head domain of myosin shown in its relation to the actin filament. The NH2-terminal end of the myosin heavy chain is in the globular head. The light chains bind to the neck region of the MHC. In this figure, the orientation of the myosin to the actin is that of the rigor bond, i.e., at the end of the power stroke. [From M. Irving and G. Piazzesi, Motions of myosin heads that drive muscle contraction. News Physiol. Sci. 12(6), 249-254 (December 1997).]... [Pg.461]

Nilson BH, Solomon A, Bjorck L, Akerstrom B Protein L from Peptostreptococcus magnus binds to the kappa light chain variable domain. J Biol Chem 1992 267 2234-2239. [Pg.103]

Kinesins (20) ATP Eleavy and light chains head domains with ATPase activity and microtubule-binding site Cytoplasm Transport of cargo vesicles and chromosomes during mitosis... [Pg.80]

Figure 14.15 Stmcture of the SI fragment of chicken myosin as a Richardson diagram (a) and a space-filling model (b). The two light chains are shown in magenta and yellow. The heavy chain is colored according to three proteolytic fragments produced by trypsin a 25-kDa N-terminal domain (green) a central 50-kDa fragment (red) divided by a cleft into a 50K upper and a 50K lower domain and a 20-kDa C-terminal domain (blue) that links the myosin head to the coiled-coil tail. The 50-kDa and 20-kDa domains both bind actin, while the 25-kDa domain binds ATP. [(b) Courtesy of 1. Rayment.]... Figure 14.15 Stmcture of the SI fragment of chicken myosin as a Richardson diagram (a) and a space-filling model (b). The two light chains are shown in magenta and yellow. The heavy chain is colored according to three proteolytic fragments produced by trypsin a 25-kDa N-terminal domain (green) a central 50-kDa fragment (red) divided by a cleft into a 50K upper and a 50K lower domain and a 20-kDa C-terminal domain (blue) that links the myosin head to the coiled-coil tail. The 50-kDa and 20-kDa domains both bind actin, while the 25-kDa domain binds ATP. [(b) Courtesy of 1. Rayment.]...

See other pages where Light-chain binding domain is mentioned: [Pg.62]    [Pg.328]    [Pg.916]    [Pg.583]    [Pg.886]    [Pg.21]    [Pg.62]    [Pg.328]    [Pg.916]    [Pg.583]    [Pg.886]    [Pg.21]    [Pg.60]    [Pg.233]    [Pg.234]    [Pg.136]    [Pg.46]    [Pg.25]    [Pg.310]    [Pg.394]    [Pg.255]    [Pg.438]    [Pg.1511]    [Pg.221]    [Pg.980]    [Pg.1068]    [Pg.38]    [Pg.794]    [Pg.41]    [Pg.305]    [Pg.273]    [Pg.208]    [Pg.211]    [Pg.294]    [Pg.303]    [Pg.304]    [Pg.305]    [Pg.306]    [Pg.306]    [Pg.317]    [Pg.601]    [Pg.62]    [Pg.70]   
See also in sourсe #XX -- [ Pg.328 , Pg.329 ]




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