Structure, regulation, and mechanisms of nonmuscle myosin-2

Figures

• 

  Fig. 1. Heavy chain domain organization and structural conservation of human NM2 paralogs a. Heavy chain domain organization of a generic human NM2 paralog featuring an N-terminal motor domain (pink), a central neck domain that contains two IQ motifs (grey), and a C-terminal tail domain (green). Schematic not drawn to scale. b, Percent identity matrix summarizes the degree of identity between the heavy chains of human NM2 paralogs (left), the motor domain (middle) and the tail domain (right). c, Consurf analysis [197] shows the conservation of amino acid positions in the structure of the NM2C motor domain (PDB ID: 5I4E). Views are rotated by 180º

• 

  Fig. 2. Structural features of the motor domain and kinetic cycle of the NM2s a. Key structural features of the myosin motor domain of NM2 paralogs (PDB ID: 5I4E). The myosin motor domain is shown in cartoon representation, the bound nucleotide in spheres. Mg2+ is shown as green sphere. Light chains are not shown for clarity. b, Key structural features in the nucleotide binding pocket of NM2 paralogs (PDB ID: 5I4E). The myosin motor domain is shown in cartoon representation, the bound nucleotide in stick representation, and Mg2+ is shown as green sphere. c, Allocation of structural states to the minimal kinetic scheme of the actomyosin ATPase cycle. The myosin motor domain (pink) is shown in surface representation, actin is shown in flat surface representation (grey). Light chains are not shown for clarity. Schematic not drawn to scale

• 

  Fig. 3. Regulation mechanisms of NM2. Select regulation mechanisms of NM2s reviewed in this work. Grey and red font colors indicate regulation mechanisms specific for NM2A and NM2B, respectively. Dashed lines indicate putative regulation mechanisms. Force: force dependent maturation of heterotypic filaments