[HTML][HTML] Mechanism and specificity of pentachloropseudilin-mediated inhibition of myosin motor activity
Here, we report that the natural compound pentachloropseudilin (PClP) acts as a reversible
and allosteric inhibitor of myosin ATPase and motor activity. IC 50 values are in the range
from 1 to 5 μm for mammalian class-1 myosins and greater than 90 μm for class-2 and class-
5 myosins, and no inhibition was observed with class-6 and class-7 myosins. We show that
in mammalian cells, PClP selectively inhibits myosin-1c function. To elucidate the structural
basis for PClP-induced allosteric coupling and isoform-specific differences in the inhibitory …
and allosteric inhibitor of myosin ATPase and motor activity. IC 50 values are in the range
from 1 to 5 μm for mammalian class-1 myosins and greater than 90 μm for class-2 and class-
5 myosins, and no inhibition was observed with class-6 and class-7 myosins. We show that
in mammalian cells, PClP selectively inhibits myosin-1c function. To elucidate the structural
basis for PClP-induced allosteric coupling and isoform-specific differences in the inhibitory …