Crystal structure of RhoA-GDP and its functional implications.
RhoA, a ubiquitous intracellular GTPase, mediates cytoskeletal responses to extracellular signals. A 2.1 A resolution crystal structure of the human RhoA-GDP complex shows unique stereochemistry in the switch I region, which results in a novel mode of Mg2+ binding.
Wei
Y
Y
Zhang
Y
Y
Derewenda
U
U
Liu
X
X
Minor
W
W
Nakamoto
R K
RK
Somlyo
A V
AV
Somlyo
A P
AP
Derewenda
Z S
ZS
D018360:Crystallography, X-Ray; D019204:GTP-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D006153:Guanosine Diphosphate / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008274:Magnesium / Q000737:chemistry; D008958:Models, Molecular; D011487:Protein Conformation; D020742:rhoA GTP-Binding Protein
D006153:Guanosine Diphosphate; D019204:GTP-Binding Proteins; D020742:rhoA GTP-Binding Protein; D008274:Magnesium