title: Probing the transducin nucleotide binding site with GDP analogues.
abstract: An affinity study between the G protein of the visual photoreceptor, transducin, and eight different non-hydrolyzable GDP analogues is described. Imidodiphosphate derivatives have been shown to exhibit good affinities to transducin. This very important heterotrimeric G protein is shown to be highly restrictive with regard to structural modifications of the nucleotide at the pyrophosphate moiety, at the 3' position on ribose, as well as at the N1 position of the purine.
authors.affiliation: Laboratoire de Synthèse Bioorganique associé au CNRS, Université Louis Pasteur, Illkirch, France.
authors.forename: S P
authors.initials: SP
authors.lastname: Vincent
authors.forename: S
authors.initials: S
authors.lastname: Grenier
authors.forename: C
authors.initials: C
authors.lastname: Mioskowski
authors.forename: C
authors.initials: C
authors.lastname: Salesse
authors.forename: L
authors.initials: L
authors.lastname: Lebeau
mesh_terms: D001665:Binding Sites / Q000187:drug effects; D006153:Guanosine Diphosphate / Q000031:analogs & derivatives* / Q000494:pharmacology*; D007094:Imides / Q000737:chemistry; D008024:Ligands; D013329:Structure-Activity Relationship; D015293:Transducin / Q000737:chemistry / Q000187:drug effects*
chemical_list: D007094:Imides; D008024:Ligands; D006153:Guanosine Diphosphate; D015293:Transducin