Members of the Rho family of small G proteins transduce signals from plasma-membranereceptors and control cell adhesion, motility and shape by actin cytoskeleton formation.Like all other GTPases, Rho proteins act as molecular switches, with an activeGTP-bound form and an inactive GDP-bound form. The active conformation is promoted byguanine-nucleotide exchange factors, and the inactive state by GTPase-activating proteins(GAPs) which stimulate the intrinsic GTPase activity of small G proteins.This entry is a Rho/Rac/Cdc42-like GAP domain, that is found in a wide variety of large,multi-functional proteins [<cite idref="PUB00004251"/>].A number of structure are known for this family[<cite idref="PUB00004251"/>, <cite idref="PUB00004880"/>, <cite idref="PUB00004258"/>].The domain is composed of seven alpha helices.This domain is also known as the breakpoint cluster region-homology (BH) domain.