Structures of the human eIF4E homologous protein, h4EHP, in its m7GTP-bound and unliganded forms.
|Abstract||All eukaryotic cellular mRNAs contain a 5' m(7)GpppN cap. In addition to conferring stability to the mRNA, the cap is required for pre-mRNA splicing, nuclear export and translation by providing an anchor point for protein binding. In translation, the interaction between the cap and the eukaryotic initiation factor 4E (eIF4E) is important in the recruitment of the mRNAs to the ribosome. Human 4EHP (h4EHP) is a homologue of eIF4E. Like eIF4E it is ... [truncated at 450 characters in length]|
|Author||Rosettani, Pamela; Knapp, Stefan; Vismara, Maria-Grazia; et al|
|Subject||Amino Acid Sequence Binding Sites Calorimetry Conserved Sequence Crystallography, X-Ray Eukaryotic Initiation Factor-4E Evolution, Molecular Guanosine Triphosphate Humans Models, Molecular Molecular Sequence Data Mutation Peptides Protein Binding RNA Cap-Binding Proteins RNA Caps chemistry genetics metabolism chemistry metabolism chemistry chemistry genetics metabolism chemistry|
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|
Superfamilies SDR and MDR: from early ancestry to present forms. Emergence of three lines, a Zn-metalloenzyme, and distinct variabilities.
|Abstract||Two large gene and protein superfamilies, SDR and MDR (short- and medium-chain dehydrogenases/reductases), were originally defined from analysis of alcohol and polyol dehydrogenases. The superfamilies contain minimally 82 and 25 genes, respectively, in humans, minimally 324 and 86 enzyme families when known lines in other organisms are also included, and over 47,000 and 15,000 variants in existing sequence data bank entries. SDR enzymes have one- ... [truncated at 450 characters in length]|
|Author||Jörnvall, Hans; Hedlund, Joel; Bergman, Tomas; et al|
|Subject||Acyl-CoA Dehydrogenase Butyryl-CoA Dehydrogenase Evolution, Molecular Humans Metalloproteins Phylogeny Protein Conformation Zinc chemistry classification genetics chemistry classification genetics chemistry classification genetics metabolism|
Identification of macrodomain proteins as novel O-acetyl-ADP-ribose deacetylases.
|Abstract||Sirtuins are a family of protein lysine deacetylases, which regulate gene silencing, metabolism, life span, and chromatin structure. Sirtuins utilize NAD(+) to deacetylate proteins, yielding O-acetyl-ADP-ribose (OAADPr) as a reaction product. The macrodomain is a ubiquitous protein module known to bind ADP-ribose derivatives, which diverged through evolution to support many different protein functions and pathways. The observation that some sirtu ... [truncated at 450 characters in length]|
|Author||Chen, Dawei; Vollmar, Melanie; Rossi, Marianna N; et al|
|Subject||Escherichia coli Escherichia coli Proteins Evolution, Molecular Fungal Proteins Hela Cells Humans Neurospora crassa Protein Structure, Tertiary Sirtuins Staphylococcus aureus enzymology genetics chemistry genetics metabolism chemistry genetics metabolism enzymology genetics chemistry genetics metabolism enzymology genetics|