TABLE 3.

Comparison of IC₅₀ values and blebbistatin binding site residues of nonmuscle myosin-2s from selected model organisms

	Drosophila nonmuscle myosin-2	Drosophila nonmuscle myosin-2 M466I	Acanthamoeba nonmuscle myosin-2	Dictyostelium nonmuscle myosin-2	Human nonmuscle myosin-2A	Blebbistatin interaction
IC50 (µM)	>>200	36.3	83 (14)	4.9 (14)	5.1 (14)
Residue	Leu271	Leu271	Leu262	Leu262	Leu258	Benzyl ring
Residue	Phe477	Phe477	Phe468	Phe466	Phe464	Benzyl ring
Residue	Glu478	Glu478	Glu469	Glu467	Glu465	Benzyl ring
Residue	Val651	Val651	Val652	Val630	Val646	Benzyl ring
Residuea	Ala467	Ala467	Ser458	Ser456	Ala454	Tetrahydropyrrolo ring
Residue	Ile482	Ile482	Ile473	Ile471	Ile469	Tetrahydropyrrolo ring
Residue	Thr485	Thr485	Thr476	Thr474	Thr472	Methylquinolinone
Residue	Tyr655	Tyr655	Tyr656	Tyr634	Tyr650	Methylquinolinone
Residue	Gln658	Gln658	Gln659	Gln637	Gln653	Methylquinolinone
Residue	Leu662	Leu662	Leu663	Leu641	Leu657	Methylquinolinone
Residuea	Met466	Ile466	Ile459	Ile457	Ile455	None

Reference binding site residues were previously described for the Dictyostelium nonmuscle myosin-2/blebbistatin complex by Allingham et al. (29). Residues corresponding to Drosophila nonmuscle myosin-2 Met466 are listed for completeness. ^aDeviations in the amino acid sequence.