title: Crystal structure of RhoA-GDP and its functional implications.
abstract: 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.
authors.forename: Y
authors.initials: Y
authors.lastname: Wei
authors.forename: Y
authors.initials: Y
authors.lastname: Zhang
authors.forename: U
authors.initials: U
authors.lastname: Derewenda
authors.forename: X
authors.initials: X
authors.lastname: Liu
authors.forename: W
authors.initials: W
authors.lastname: Minor
authors.forename: R K
authors.initials: RK
authors.lastname: Nakamoto
authors.forename: A V
authors.initials: AV
authors.lastname: Somlyo
authors.forename: A P
authors.initials: AP
authors.lastname: Somlyo
authors.forename: Z S
authors.initials: ZS
authors.lastname: Derewenda
mesh_terms: 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
chemical_list: D006153:Guanosine Diphosphate; D019204:GTP-Binding Proteins; D020742:rhoA GTP-Binding Protein; D008274:Magnesium