Tropomyosin binds to actin filaments through a 'Gestalt-binding' mechanism, relying on the form-fitting complementarity of the entire acto-tropomyosin system rather than strong stereo-specific interactions.
We argue that the overall behavior of tropomyosin on F-actin cannot be easily discerned by examining thin filaments reduced to their smallest interacting units. In isolation, the individual interactions of actin and tropomyosin, by themselves, are too weak to account for the specificity of the system. Instead the association of tropomyosin on actin can only be fully explained after considering the concerted action of the entire acto-tropomyosin system. We propose that the low K ( a ) describing tropomyosin:actin interaction, when taken together with the form-fitting complementarity of tropomyosin strands on F-actin and the tendency for tropomyosin to polymerize end-to-end, make possible unique thin filament functions both locally and at higher levels of filament organization.
Holmes et al. (Mon,) reported a review. Tropomyosin binds to actin filaments through a 'Gestalt-binding' mechanism, relying on the form-fitting complementarity of the entire acto-tropomyosin system rather than strong stereo-specific interactions.