Larger than Dbl: new structural insights into RhoA activation.
Dbl homology (DH) domains are almost always followed immediately by pleckstrin homology (PH) domains in Dbl family proteins, and these DH-PH fragments directly activate GDP-bound Rho GTPases by catalyzing the exchange of GDP for GTP. New crystal structures of the DH-PH domains from leukemia-associated Rho guanine nucleotide exchange factor (RhoGEF) and PDZ-RhoGEF bound to RhoA reveal how DH-PH domains cooperate to specifically activate Rho GTPases.
Rossman
Kent L
KL
Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Sondek
John
J
D004789:Enzyme Activation; D008958:Models, Molecular; D009712:Nucleotides, Cyclic / Q000378:metabolism; D017434:Protein Structure, Tertiary; D020742:rhoA GTP-Binding Protein / Q000737:chemistry* / Q000378:metabolism*
D009712:Nucleotides, Cyclic; D020742:rhoA GTP-Binding Protein