Characterization of human DHRS6, an orphan short chain dehydrogenase/reductase enzyme: a novel, cytosolic type 2 R-beta-hydroxybutyrate dehydrogenase.
|Abstract||Human DHRS6 is a previously uncharacterized member of the short chain dehydrogenases/reductase family and displays significant homologies to bacterial hydroxybutyrate dehydrogenases. Substrate screening reveals sole NAD(+)-dependent conversion of (R)-hydroxybutyrate to acetoacetate with K(m) values of about 10 mm, consistent with plasma levels of circulating ketone bodies in situations of starvation or ketoacidosis. The structure of human DHRS6 w ... [truncated at 450 characters in length]|
|Author||Guo, Kunde; Lukacik, Petra; Papagrigoriou, Evangelos; et al|
|Subject||Amino Acid Motifs Amino Acid Sequence Animals Arginine Binding Sites Cloning, Molecular Crystallography, X-Ray Cytosol Dose-Response Relationship, Drug Exons Green Fluorescent Proteins Hela Cells Humans Hydrogen-Ion Concentration Hydroxybutyrate Dehydrogenase Kinetics Lipids Mitochondria Models, Molecular Molecular Sequence Data Oxidoreductases Phylogeny Protein Conformation Protein Folding Protein Structure, Tertiary Sequence Homology, Amino Acid Substrate Specificity Sulfates chemistry enzymology metabolism metabolism chemistry genetics chemistry metabolism chemistry chemistry|
Structure and substrate specificity of the Pim-1 kinase.
|Abstract||The Pim kinases are a family of three vertebrate protein serine/threonine kinases (Pim-1, -2, and -3) belonging to the CAMK (calmodulin-dependent protein kinase-related) group. Pim kinases are emerging as important mediators of cytokine signaling pathways in hematopoietic cells, and they contribute to the progression of certain leukemias and solid tumors. A number of cytoplasmic and nuclear proteins are phosphorylated by Pim kinases and may act a ... [truncated at 450 characters in length]|
|Author||Bullock, Alex N; Debreczeni, Judit; Amos, Ann L; et al|
|Subject||Amino Acid Motifs Arginine Binding Sites Biotinylation Calcium-Calmodulin-Dependent Protein Kinase Type 1 Calcium-Calmodulin-Dependent Protein Kinases Calorimetry Cell Nucleus Crystallography, X-Ray Cytoplasm Glycine Hematopoietic Stem Cells Humans Kinetics Models, Molecular Peptide Library Peptide Nucleic Acids Peptides Phosphorylation Protein Binding Protein Conformation Protein Isoforms Protein Structure, Tertiary Protein-Serine-Threonine Kinases Proto-Oncogene Proteins Proto-Oncogene Proteins c-pim-1 Substrate Specificity chemistry metabolism metabolism metabolism chemistry metabolism chemistry chemistry metabolism physiology physiology metabolism physiology|
Structure of the human RECQ1 helicase reveals a putative strand-separation pin.
|Abstract||RecQ-like helicases, which include 5 members in the human genome, are important in maintaining genome integrity. We present a crystal structure of a truncated form of the human RECQ1 protein with Mg-ADP. The truncated protein is active in DNA fork unwinding but lacks other activities of the full-length enzyme: disruption of Holliday junctions and DNA strand annealing. The structure of human RECQ1 resembles that of Escherichia coli RecQ, with some ... [truncated at 450 characters in length]|
|Author||Pike, Ashley C W; Shrestha, Binesh; Popuri, Venkateswarlu; et al|
|Subject||Adenosine Diphosphate Adenosine Triphosphate Amino Acid Motifs Amino Acid Sequence Conserved Sequence DNA Escherichia coli Humans Kinetics Molecular Sequence Data Mutant Proteins Protein Binding Protein Structure, Tertiary RecQ Helicases Sequence Alignment Zinc metabolism metabolism enzymology chemistry chemistry metabolism metabolism|
Linear motif atlas for phosphorylation-dependent signaling.
|Abstract||Systematic and quantitative analysis of protein phosphorylation is revealing dynamic regulatory networks underlying cellular responses to environmental cues. However, matching these sites to the kinases that phosphorylate them and the phosphorylation-dependent binding domains that may subsequently bind to them remains a challenge. NetPhorest is an atlas of consensus sequence motifs that covers 179 kinases and 104 phosphorylation-dependent binding ... [truncated at 450 characters in length]|
|Author||Miller, Martin Lee; Jensen, Lars Juhl; Diella, Francesca; et al|
|Subject||14-3-3 Proteins Amino Acid Motifs Animals BRCA1 Protein Consensus Sequence Databases, Protein Humans Phosphorylation Phosphotransferases Phosphotyrosine Protein Binding Signal Transduction src Homology Domains chemistry chemistry chemistry metabolism|
Structural basis for Par-4 recognition by the SPRY domain- and SOCS box-containing proteins SPSB1, SPSB2, and SPSB4.
|Abstract||The mammalian SPRY domain- and SOCS box-containing proteins, SPSB1 to SPSB4, belong to the SOCS box family of E3 ubiquitin ligases. Substrate recognition sites for the SPRY domain are identified only for human Par-4 (ELNNNL) and for the Drosophila orthologue GUSTAVUS binding to the DEAD-box RNA helicase VASA (DINNNN). To further investigate this consensus motif, we determined the crystal structures of SPSB1, SPSB2, and SPSB4, as well as their bin ... [truncated at 450 characters in length]|
|Author||Filippakopoulos, Panagis; Low, Andrew; Sharpe, Timothy D; et al|
|Subject||Amino Acid Motifs Amino Acid Sequence Animals Binding Sites Consensus Sequence Crystallography, X-Ray DEAD-box RNA Helicases Humans Magnetic Resonance Spectroscopy Mice Protein Binding Protein Conformation Receptors, Thrombin Suppressor of Cytokine Signaling Proteins chemistry metabolism chemistry metabolism chemistry metabolism|