Key result
The filamin sequence 121-147, particularly the hydrophobic 141-147 region, constitutes the main interface for interaction with actin, alongside additional hydrophilic regions.
Population
Smooth muscle filamin and filamentous actin (in vitro biochemical model)
Comparison
Enzymatic digestion, cross-reactive anti-peptide… vs alpha-actinin
Design
Preclinical
Authors
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Provides molecular detail on filamin-actin binding; hypothesis-generating for cytoskeletal regulation in vascular disease.
The study identifies the 121-147 sequence of smooth muscle filamin as the primary binding interface with actin, highlighting both similarities and distinct differences compared to alpha-actinin.
Lebart et al. (1994) studied this question. Filamin NH2-terminal fragment was evaluated on Interaction with filamentous actin. The filamin sequence 121-147, particularly the hydrophobic 141-147 region, constitutes the main interface for interaction with actin, alongside additional hydrophilic regions.
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