Structural changes during ion channel gating.
|Abstract||Ion channels are generally multi-subunit complexes, with the ion conduction pathway formed at the subunit interface. In moving between the closed and open states, three structurally distinct channels, represented by the recently determined structures of a mechanosensitive, ligand-gated and K(+) selective channel, all move transmembrane helices away from the central ion conduction pathway. In all three cases, this results in the displacement of a ... [truncated at 450 characters in length]|
|Author||Doyle, Declan A;|
|Subject||Amino Acid Sequence Animals Crystallography, X-Ray Humans Ion Channel Gating Ion Channels Potassium Channels Protein Folding Protein Structure, Quaternary Protein Structure, Secondary physiology chemistry metabolism chemistry metabolism|
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|
Thermal unfolding of the archaeal DNA and RNA binding protein Ssh10.
|Abstract||The reversible thermal unfolding of the archaeal histone-like protein Ssh10b from the extremophile Sulfolobus shibatae was studied using differential scanning calorimetry and circular dichroism spectroscopy. Analytical ultracentrifugation and gel filtration showed that Ssh10b is a stable dimer in the pH range 2.5-7.0. Thermal denaturation data fit into a two-state unfolding model, suggesting that the Ssh10 dimer unfolds as a single cooperative un ... [truncated at 450 characters in length]|
|Author||Wu, Xiaoqiu; Oppermann, Madalina; Berndt, Kurt D; et al|
|Subject||Amino Acid Sequence Archaeal Proteins Calorimetry, Differential Scanning Circular Dichroism DNA-Binding Proteins Histones Hot Temperature Hydrogen-Ion Concentration Molecular Sequence Data Protein Denaturation Protein Folding RNA-Binding Proteins Sulfolobus Thermodynamics chemistry metabolism chemistry metabolism chemistry metabolism chemistry metabolism metabolism|
Structure of the pseudokinase VRK3 reveals a degraded catalytic site, a highly conserved kinase fold, and a putative regulatory binding site.
|Abstract||About 10% of all protein kinases are predicted to be enzymatically inactive pseudokinases, but the structural details of kinase inactivation have remained unclear. We present the first structure of a pseudokinase, VRK3, and that of its closest active relative, VRK2. Profound changes to the active site region underlie the loss of catalytic activity, and VRK3 cannot bind ATP because of residue substitutions in the binding pocket. However, VRK3 stil ... [truncated at 450 characters in length]|
|Author||Scheeff, Eric D; Eswaran, Jeyanthy; Bunkoczi, Gabor; et al|
|Subject||Adenosine Triphosphate Amino Acid Sequence Binding Sites Catalytic Domain Models, Molecular Molecular Sequence Data Phosphotransferases Protein Conformation Protein Folding metabolism chemistry metabolism|
SGC--structural biology and human health: a new approach to publishing structural biology results.
|Author||Lee, Wen Hwa; Atienza-Herrero, Julián; Abagyan, Ruben; et al|
|Subject||Amino Acid Sequence Computational Biology Databases, Protein Genomics Humans Protein Conformation Protein Folding Proteins Publishing Structural Homology, Protein economics methods chemistry classification genetics|