Phosphorylated Smooth Muscle Heavy Meromyosin Shows an Open Conformation Linked to Activation

Smooth muscle myosin and smooth muscle heavy meromyosin (smHMM) are activated by regulatory light chain phosphorylation, but the mechanism remains unclear. Dephosphorylated, inactive smHMM assumes a closed conformation with asymmetric intramolecular head–head interactions between motor domains. The...

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Veröffentlicht in:	Journal of molecular biology 2012-01, Vol.415 (2), p.274-287
Hauptverfasser:	Baumann, Bruce A.J., Taylor, Dianne W., Huang, Zhong, Tama, Florence, Fagnant, Patricia M., Trybus, Kathleen M., Taylor, Kenneth A.
Format:	Artikel
Sprache:	eng
Schlagworte:	2D crystalline arrays actin Animals chemistry Chickens crystallography Crystallography - methods electron crystallography heavy meromyosin lipid monolayers metabolism methods Models, Biological Models, Molecular Muscle, Smooth Muscle, Smooth - chemistry Muscle, Smooth - metabolism myosin light chains myosin regulation Myosin Subfragments Myosin Subfragments - chemistry Myosin Subfragments - metabolism Phosphorylation Protein Binding Protein Conformation smooth muscle
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