Key result
The conformation of Z-repeat 7 of titin complexed with alpha-actinin was found to be helical, suggesting a binding mode similar to troponin I to troponin C.
Population
In vitro protein complexes of titin Z-repeat 7 and the 73-amino acid C-terminal portion of alpha-actinin
Design
Preclinical
Authors
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Provides structural hypothesis for titin–α-actinin interaction; leaves open relevance to human cardiac Z-disk function and disease.
The interaction between titin and alpha-actinin in the Z-disk utilizes a binding mode similar to troponin I and troponin C, highlighting a general alternative binding mechanism for calmodulin-like domains.
Atkinson et al. (2000) studied this question. The conformation of Z-repeat 7 of titin complexed with alpha-actinin was found to be helical, suggesting a binding mode similar to troponin I to troponin C.
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