<p>Members of Rho are small G proteins that transduce signals from plasma-membrane receptors and control cell adhesion, motility and shape by actin cytoskeleton formation. Like all other GTPases, Rho proteins act as molecular switches, with an active GTP-bound form and an inactive GDP-bound form. The active conformation is promoted by guanine-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 which is found in a wide variety of large, multi-functional proteins [<cite idref="PUB00004251"/>]. A number of structures are known [<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.</p> <p>RhoGAP is widely evolutionarily conserved from <taxon tax_id="4932">Saccharomyces cerevisiae</taxon> (Baker's yeast) to <taxon tax_id="9606">Homo sapiens</taxon> (Human).</p>