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Structure of vertebrate myosin filaments

The skeletal and cardiac muscles of vertebrates are important because of their relevance to human physiology and disease. However, vertebrate filaments are more challenging to study than invertebrates, as they are less stable and more complex (with proteins in addition to myosin, e.g. titin, MyBP-C). Using single particle techniques and negative staining we determined the organization of the myosin heads, titin, and MyBP-C (Zoghbi et al., 2008) in mouse cardiac filaments. The myosin heads have a similar interacting-head structure to that in invertebrates (left figure), although the interaction is less stable. The reconstruction also shows the layout of the giant protein, titin (blue beads in right figure), running along the filament surface between the myosin heads (green), and the organization of MyBP-C’s C-terminal domains (orange), binding to the filament backbone. Our current goal is to obtain high resolution reconstructions of vertebrate filaments (both skeletal and cardiac) by cryo-EM.

Craig Lab - UMMS - vertabrate fillament recon