title: A new tool for G protein analysis.
abstract: G proteins play a pivotal role in cellular signaling by acting as molecular switches that undergo conformational changes upon binding GTP. The primary sequence constituting the binding cleft among the >160 G proteins in the human genome is highly conserved, consistent with the fact that these proteins share similar guanine nucleotide-binding characteristics. Recent work has demonstrated the feasibility of designing new analogs of GTP that can specifically activate G proteins whose nucleotide-binding sites have been remodeled through mutagenesis. This strategy has the potential to provide new insights into how G proteins act as molecular switches that engage their downstream target/effector proteins to generate specific signaling outputs.
authors.affiliation: Department of Molecular Medicine, Cornell University, Ithaca, New York 14853-6401, USA.
authors.forename: Jon W
authors.initials: JW
authors.lastname: Erickson
authors.forename: Richard A
authors.initials: RA
authors.lastname: Cerione
mesh_terms: D001665:Binding Sites; D019204:GTP-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008024:Ligands; D008958:Models, Molecular; D016296:Mutagenesis; D011485:Protein Binding; D011487:Protein Conformation; D015398:Signal Transduction; D054852:Small Molecule Libraries / Q000737:chemistry*
chemical_list: D008024:Ligands; D054852:Small Molecule Libraries; D019204:GTP-Binding Proteins