The centaurin gamma-1 GTPase-like domain functions as an NTPase.
|Abstract||Centaurins are a family of proteins that contain GTPase-activating protein domains, with the gamma family members containing in addition a GTPase-like domain. Centaurins reside mainly in the nucleus and are known to activate phosphoinositide 3-kinase, a key regulator of cell proliferation, motility and vesicular trafficking. In the present study, using X-ray structural analysis, enzymatic assays and nucleotide-binding studies, we show that, for C ... [truncated at 450 characters in length]|
|Author||Soundararajan, Meera; Yang, Xiaowen; Elkins, Jonathan M; et al|
|Subject||Amino Acid Sequence Binding Sites Cloning, Molecular Escherichia coli GTP-Binding Proteins GTPase-Activating Proteins Hydrolysis Models, Molecular Molecular Structure Nucleoside-Triphosphatase Nucleotides Protein Structure, Tertiary Signal Transduction Substrate Specificity ras Proteins metabolism chemistry metabolism chemistry metabolism chemistry metabolism metabolism chemistry metabolism|
RhoB can adopt a Mg2+ free conformation prior to GEF binding.
|Author||Soundararajan, Meera; Turnbull, Andrew; Fedorov, Oleg; et al|
|Subject||Enzyme Stability Guanine Nucleotide Exchange Factors Hydrolysis Magnesium Models, Molecular Protein Binding Protein Structure, Secondary rhoA GTP-Binding Protein rhoB GTP-Binding Protein drug effects metabolism drug effects metabolism pharmacology drug effects chemistry chemistry 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|