A regular pattern of two types of 100-residue motif in the sequence of titin

@article{Labeit1990ARP,
  title={A regular pattern of two types of 100-residue motif in the sequence of titin},
  author={Siegfried Labeit and Denise P. Barlow and Mathias Gautel and Toby J. Gibson and John C. Holt and C. L. Hsieh and Uta Francke and Kevin R. Leonard and John Wardale and A. Whiting and J. Trinick},
  journal={Nature},
  year={1990},
  volume={345},
  pages={273-276}
}
TITIN is the largest polypeptide yet described (relative molecular mass ˜3xl06; refs 1,2) and an abundant protein of striated muscle3. Its molecules are string-like4 and in vivo span from the M to Z-lines5,6. I-band regions of titin are thought to make elastic connections between the thick filament and the Z-line5–7, thereby forming a third type of sarcomere filament8,9. These would centre the A-band in the sarcomere and provide structural continuity in relaxed myofibrils10. The A-band region… 
Dissecting titin into its structural motifs: identification of an alpha-helix motif near the titin N-terminus.
TLDR
A study of a stretch located in the titin N-terminus and part of a linker between two modules is presented, drawn toward this region because it shows 100% probability to form a coiled coil when analyzed by a prediction program.
The Axial Alignment of Titin on the Muscle Thick Filament Supports Its Role as a Molecular Ruler
Modularity and homology: modelling of the titin type I modules and their interfaces.
TLDR
Results from homology modelling the whole family of Fn3 domains in titin suggest residues that contribute to the fold stability and allow us to distinguish these from residues likely to have functional importance and suggest putative surfaces of interaction with other proteins.
1H and 15N NMR resonance assignments and secondary structure of titin type I domains
TLDR
It is shown that the type I domains of titin have the Fn3 fold as proposed, consisting of a three- and a four-stranded β-sheet, and 8 out of 10 prolines are found on the sameside of the molecule and form an exposed hydrophobic patch.
The assembly of immunoglobulin-like modules in titin: implications for muscle elasticity.
TLDR
By a combined approach making use of small angle X-ray scattering and nuclear magnetic resonance techniques, the questions of what are the average mutual orientation of poly-Igs and the degree of flexibility around the domain interfaces are addressed and titin behaves as a row of beads connected by rigid hinges.
Immunoglobulin-type domains of titin: same fold, different stability?
TLDR
The stability of the modules over a range of conditions was investigated by measuring key thermodynamic parameters for both thermal and chemical denaturation and by monitoring amide proton exchange as a function of time.
The globular head domain of titin extends into the center of the sarcomeric M band. cDNA cloning, epitope mapping and immunoelectron microscopy of two titin-associated proteins.
TLDR
By monoclonal antibodies, cDNA cloning and immunoelectron microscopy the two titin-associated proteins (190 and 165 kDa proteins), which seem responsible for the formation of a head structure on one end of the 0.9 micron long titin string, are characterized.
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References

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TLDR
Results indicate that the amino acid sequence of smMLCK encodes multiple functional motifs in addition to the catalytic domain, which is defined as being contained within and probably identical to the pseudosubstrate domain.
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TLDR
The recognition of the existence of two sets of sarcomere-associated cytoskeletal filaments within adult striated muscle fibers may be a significant step toward resolving some of the unsettled questions in muscle mechanics such as those that have been discussed in this meeting.
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TLDR
Both of the cAMP-dependent protein kinase phosphorylation sites were identified by sequence homology and a linear model for MLCK is presented placing the various domains in relative position.
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TLDR
Studies of electrophoretic mobility on 2-3% polyacrylamide gel electrophoresis, amino acid composition, and localization in myofibrils determined by the indirect immunofluorescence technique showed that titin and connectin are identical.
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TLDR
Tin molecules appear as polar structures lacking over large regions repetitive epitopes over half-sarcomere lengths, and one physical end seems related to Z line anchorage, while the other may bind close to the M line.
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TLDR
Homologies of the sequence of twit-chin have unexpected similarities to the sequences of proteins of the immunoglobulin superfamily, cell adhesion molecules and vertebrate muscle proteins, including myosin light-chain kinase, which indicate that the protein is involved in a novel mechanism of myOSin regulation.
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TLDR
It can be confirmed that a 81 molecule interacts morphologically with actin at two sites, and the major domains A, B and D split into two domains, i.e. into Ai and A2, Hi and B2, and Dl and D2 respectively.
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