Key result
Insertion of the SAH domain into a truncated myosin 5a lever restored its powerstroke to 21.5 nm, close to the wild-type 25.2 nm, demonstrating that SAH domains can act as functional levers.
Population
Mouse myosin 5a (Myo5) constructs
Comparison
Replacement of four of the six… vs Wild-type Myo5 and truncated Myo5
Design
Preclinical
Authors
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SAH domains may serve as myosin levers in model systems; leaves open their relevance to cardiac myosins or human disease.
Absolute Event Rate: 21.5% vs 25.2%
The SAH domain can act as a stiff structural extension to form part of a functional lever in myosins, suggesting a broader structural role in other proteins.
Baboolal et al. (2009) studied this question. Myo5-2IQ-SAH chimera vs. Myo5-6IQ (wild-type) and Myo5-2IQ was evaluated on Powerstroke size. Insertion of the SAH domain into a truncated myosin 5a lever restored its powerstroke to 21.5 nm, close to the wild-type 25.2 nm, demonstrating that SAH domains can act as functional levers.