Explore: Gtpases

highly conserved P-loop "G domain", a protein domain common to many GTPases. GTPases function as molecular switches or timers in many fundamental cellular

(GDP). The best-known members are the Ras GTPases and hence they are sometimes called as Ras superfamily GTPases. A typical G-protein is active when bound

Rac is a subfamily of the Rho family of GTPases, small (~21 kDa) signaling G proteins (more specifically a GTPase). Just as other G proteins, Rac acts as

is a single-subunit small GTPase, which is related in structure to the Gα subunit of heterotrimeric G proteins (large GTPases). G proteins function as

is a GTPase-activating protein. Furthermore, YopE is a protein domain that is a Rho GTPase-activating protein (GAP), which targets small GTPases such

small GTPases. Small GTPases act as molecular switches in intracellular signaling pathways and have many downstream targets. The most well-known GTPases comprise

larger group of enzymes called GTPases. There are two classes of G proteins. The first function as monomeric small GTPases (small G-proteins), while the

family of GTPases is a family of small (~21 kDa) signaling G proteins, and is a subfamily of the Ras superfamily. The members of the Rho GTPase family have

signaling processes functioning as a critical regulator in the activity of GTPases. GTPases act as molecular switches, cycling between an active GTP-bound state

GTPases and includes: Rnd1 Rnd2 Rnd3 (also called RhoE) Functions include downregulation of stress fibres and focal adhesions. Rho family of GTPases Ridley