Structural basis for activation of the titin kinase domain during myofibrillogenesis

Article Abstract:

Connectin, or titin, is a giant muscle protein which is important for spatial and temporal control of sarcomeres found in striated muscle. Titin kinase is the only catalytic domain of titin, and its crystal structure shows the way in which a tyrosine inhibits the active site. This tyrosine appears to be a binding partner of the substrate of titin kinase. The research shows that the titin kinase may be important in myofibrillogenesis.

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Elasticity and unfolding of single molecules of the giant muscle protein titin

Article Abstract:

The giant muscle protein titin is known for its roles in thick-filament formation and the viscoelastic properties of relaxed striated muscles. This protein, also known as connectin, is composed of tandem domains of the fibronectin and immunoglobulin types. Experiments show that the elastic properties come from two sources: from the extension of the polypeptide chain in the PEVK region and the entropy of straightening the molecule.

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Palindromic assembly of the giant muscle protein titin in the sarcomeric Z-dis

Article Abstract:

The pseudosymmetric structure of telethonin mediates a unique palindromic arrangement of two titin filaments, a type of molecular assembly previously found only in protein-DNA complexes. The unique architecture in vivo by protein complementation assays, and in vitro by experiments using fluorescence resonance energy transfer is confirmed.

United States, Science & research, Usage, Eukaryotes, Nucleotide sequence, Base sequence, Energy transformation

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