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Query: UMLS:C0271276 (Hudson)
 1,066 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Despite extensive knowledge of many muscle A-band proteins (myosin molecules, titin, C-protein (MyBP-C)), details of the organization of these molecules to form myosin filaments remain unclear. Recently the myosin head (crossbridge) configuration in a relaxed vertebrate muscle was determined from low-angle X-ray diffraction (Hudson et al. (1997), J Mol Biol 273: 440-455). This showed that, even without C-protein, the myosin head array displays a characteristic polar pattern with every third 143 A-spaced crossbridge level particularly prominent. However, X-ray diffraction cannot determine the polarity of the crossbridge array relative to the neighbouring actin filaments; information crucial to a proper understanding of the contractile event. Here, electron micrographs of negatively-stained goldfish A-segments and of fast-frozen, freeze-fractured plaice A-bands have been used to determine the resting myosin head polarity relative to the M-band. In agreement with the X-ray data, the prominent 429 A-spaced striations are seen outside the C-zone, where no non-myosin proteins apart from titin are thought to be located. The head orientation is with the concave side of the curved myosin heads (containing the entrance to the ATP-binding site) facing towards the M-band and the convex surface (containing the actin-binding region at one end) facing away from the M-band.
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PMID:A-band architecture in vertebrate skeletal muscle: polarity of the myosin head array. 1122 95

Isolated relaxed myosin filaments from the myosin-regulated scallop striated adductor muscle have been reconstructed using electron microscopy and single particle analysis of negatively stained filaments. Three-dimensional reconstruction using 7-fold rotational symmetry but without imposed helical symmetry confirmed that the myosin head array is a 7-stranded, right-handed long-pitch 24/1 helix (or left-handed short-pitch 10/1 helix) with the whole structure having an axial repeat of 1440A. Reconstruction using the full helical symmetry revealed details of the myosin head density distribution within the head crowns in the relaxed scallop myosin filament. The resulting density distribution can best be explained by an arrangement in which the two heads from the same myosin molecule interact together within each crown in a compact parallel fashion along the filament axis. The configuration is consistent with the published configuration of the two heads within vertebrate smooth muscle myosin molecules observed in two-dimensional crystals of smooth muscle myosin and in the structure of tarantula myosin filaments. All these three muscle types are myosin-regulated, providing further support for a general motif of intramolecular interacting-heads structure in the relaxed state of myosin-regulated muscles as was proposed earlier by Woodhead et al. [Woodhead, J.L., Zhao, F.-Q., Craig, R., Egelman, E.H., Alamo, L., Padron, R.. 2005. Atomic model of a myosin filament in the relaxed state. Nature 436, 1195-1199]. However, the orientation of the Wendt structure is different from that found by Woodhead in that the outer head projects outwards and the inner head lies closer to the filament backbone, as in earlier work done on the insect flight muscle myosin filaments [AL-Khayat, H.A., Hudson, L., Reedy, M.K., Irving, T.C., Squire, J.M., 2003. Myosin head configuration in relaxed insect flight muscle: X-ray modelled resting crossbridges in a pre-powerstroke state are poised for actin binding. Biophys. J. 85, 1063-1079]. Possible species specific details that may differ between the scallop and the tarantula myosin filaments are also discussed.
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PMID:The 7-stranded structure of relaxed scallop muscle myosin filaments: support for a common head configuration in myosin-regulated muscles. 1924 32