Eric H. Lee, Mu Gao, Nikos Pinotsis, Matthias Wilmanns, and Klaus Schulten.
Mechanical strength of the titin Z1Z2/telethonin complex.
Structure, 14:497-509, 2006.
LEE2006
Using molecular dynamics simulations, we have explored the
mechanical strength of the titin Z1Z2-telethonin complex, namely,
its ability to bear strong forces such as those encountered during
passive muscle stretch. Our results show that not only does this
complex resist high levels of mechanical force, suggesting that
telethonin is a major component of the N-terminal titin anchor, but
also that telethonin acts to distribute these forces between its two
joined titin Z2 domains to protect the proximal Z1 domain from
bearing too much stress. Our simulations also reveal that without
telethonin, apo-titin Z1Z2 exhibits significantly decreased
resistance to mechanical stress, and that the N-terminal segment of
telethonin (residues 1-89) does not exhibit a stable fold
conformation when it is unbound from titin Z1Z2. Consequently, our
study sheds light on a key but little studied architectural feature
of biological cells, the existence of strong mechanical links that
glue separate proteins together.
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