Resonance assignment of the RGS domain of human RGS10.
|Author||Fedorov, Oleg Y; Higman, Victoria A; Schmieder, Peter; et al|
|Subject||Carbon Isotopes Humans Nitrogen Isotopes Nuclear Magnetic Resonance, Biomolecular Protein Structure, Tertiary Protons RGS Proteins methods chemistry|
Regulator of G-protein signaling 14 (RGS14) is a selective H-Ras effector.
|Abstract||Regulator of G-protein signaling (RGS) proteins have been well-described as accelerators of Galpha-mediated GTP hydrolysis ("GTPase-accelerating proteins" or GAPs). However, RGS proteins with complex domain architectures are now known to regulate much more than Galpha GTPase activity. RGS14 contains tandem Ras-binding domains that have been reported to bind to Rap- but not Ras GTPases in vitro, leading to the suggestion that RGS14 is a Rap-specif ... [truncated at 450 characters in length]|
|Author||Willard, Francis S; Willard, Melinda D; Kimple, Adam J; et al|
|Subject||Animals Binding Sites Cell Differentiation Extracellular Signal-Regulated MAP Kinases Fibroblast Growth Factor 2 Humans Mice Mitogen-Activated Protein Kinases Multiprotein Complexes Nerve Growth Factor Neurites PC12 Cells Protein Binding RGS Proteins Rats raf Kinases ras Proteins antagonists and inhibitors physiology antagonists and inhibitors physiology physiology metabolism|
Structural determinants of G-protein alpha subunit selectivity by regulator of G-protein signaling 2 (RGS2).
|Abstract||"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 Galpha subunits (known as GTPase-accelerating protein or "GAP" activity). RGS2 is unique in its in vitro potency and selectivity as a GAP for Galpha(q) subunits. As many vasoconstrictive hormones signal via G(q) heterotrimer-coupled receptors, it is perhaps n ... [truncated at 450 characters in length]|
|Author||Kimple, Adam J; Soundararajan, Meera; Hutsell, Stephanie Q; et al|
|Subject||Binding Sites Cell Line Evolution, Molecular Fluorescence Resonance Energy Transfer GTP-Binding Protein alpha Subunits Guanosine Triphosphate Humans Hydrolysis Luminescent Proteins Models, Molecular Point Mutation Protein Binding Protein Interaction Domains and Motifs Protein Structure, Tertiary RGS Proteins Recombinant Fusion Proteins Surface Plasmon Resonance Transfection genetics genetics metabolism metabolism genetics metabolism chemistry genetics metabolism chemistry genetics metabolism|