Dynamins
dynamins
Based on domain architecture, the dynamin superfamily is broadly divided into two groups, classical dynamins and dynamin-related proteins. The common features shared by all dynamins and Drps are the presence of a large N-terminal GTPase domain, a middle domain (MD) and a GTPase effector domain (GED). While GTPase domain binds and hydrolyses GTP, MD and GED play important roles in oligomerization and regulation of GTPase activity. Classical dynamins contains two additional domains namely, pleckstrin homology domain (PHD) involved in membrane binding and a proline-rich domain (PRD) containing several SH3-binding sites important for protein–protein interactions.