Structural Determinants of G-protein α Subunit Selectivity by Regulator of G-protein Signaling 2 (RGS2)

• Published in: The Journal of biological chemistry Vol. 284; no. 29; pp. 19402 - 19411
• Main Authors: Kimple, Adam J., Soundararajan, Meera, Hutsell, Stephanie Q., Roos, Annette K., Urban, Daniel J., Setola, Vincent, Temple, Brenda R.S., Roth, Bryan L., Knapp, Stefan, Willard, Francis S., Siderovski, David P.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 17.07.2009; American Society for Biochemistry and Molecular Biology
• Subjects: Binding Sites - genetics; Cell Line; Evolution, Molecular; Fluorescence Resonance Energy Transfer; GTP-Binding Protein alpha Subunits - genetics; GTP-Binding Protein alpha Subunits - metabolism; Guanosine Triphosphate - metabolism; Humans; Hydrolysis; Luminescent Proteins - genetics; Luminescent Proteins - metabolism; Mechanisms of Signal Transduction; Models, Molecular; Point Mutation; Protein Binding; Protein Interaction Domains and Motifs; Protein Structure, Tertiary; Recombinant Fusion Proteins - chemistry; Recombinant Fusion Proteins - genetics; Recombinant Fusion Proteins - metabolism; RGS Proteins - chemistry; RGS Proteins - genetics; RGS Proteins - metabolism; Surface Plasmon Resonance; Transfection

“Regulator of G-protein signaling” (RGS) proteins facilitate the termination of G protein-coupled receptor (GPCR) signaling via their ability to increase the intrinsic GTP hydrolysis rate of Gα subunits (known as GTPase-accelerating protein or “GAP” activity). RGS2 is unique in its in vitro potency...