The crystal structure of human receptor protein tyrosine phosphatase kappa phosphatase domain 1.
|Abstract||The receptor-type protein tyrosine phosphatases (RPTPs) are integral membrane proteins composed of extracellular adhesion molecule-like domains, a single transmembrane domain, and a cytoplasmic domain. The cytoplasmic domain consists of tandem PTP domains, of which the D1 domain is enzymatically active. RPTPkappa is a member of the R2A/IIb subfamily of RPTPs along with RPTPmu, RPTPrho, and RPTPlambda. Here, we have determined the crystal structur ... [truncated at 450 characters in length]|
|Author||Eswaran, Jeyanthy; Debreczeni, Judit E; Longman, Emma; et al|
|Subject||Amino Acid Sequence Binding Sites Crystallography, X-Ray Humans Models, Molecular Molecular Sequence Data Protein Conformation Protein Structure, Tertiary Protein Tyrosine Phosphatases Receptor-Like Protein Tyrosine Phosphatases, Class 2 Sequence Homology, Amino Acid Solutions Structural Homology, Protein chemistry metabolism|
Two different conformational states of the KirBac3.1 potassium channel revealed by electron crystallography.
|Abstract||Potassium channels allow the selective flow of K(+) ions across membranes. In response to external gating signals, the potassium channel can move reversibly through a series of structural conformations from a closed to an open state. 2D crystals of the inwardly rectifying K(+) channel KirBac3.1 from Magnetospirillum magnetotacticum have been captured in two distinct conformations, providing "snap shots" of the gating process. Analysis by electron ... [truncated at 450 characters in length]|
|Author||Kuo, Anling; Domene, Carmen; Johnson, Louise N; et al|
|Subject||Amino Acid Sequence Amino Acids, Aromatic Cloning, Molecular Cryoelectron Microscopy Crystallography, X-Ray DNA, Bacterial Dimerization Lipid Bilayers Magnetospirillum Models, Molecular Molecular Sequence Data Potassium Channels, Inwardly Rectifying Protein Conformation Protein Structure, Quaternary Protein Structure, Secondary Sequence Homology, Amino Acid chemistry genetics chemistry ultrastructure|
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|
Crystal structures of mammalian glutamine synthetases illustrate substrate-induced conformational changes and provide opportunities for drug and herbicide design.
|Abstract||Glutamine synthetase (GS) catalyzes the ligation of glutamate and ammonia to form glutamine, with concomitant hydrolysis of ATP. In mammals, the activity eliminates cytotoxic ammonia, at the same time converting neurotoxic glutamate to harmless glutamine; there are a number of links between changes in GS activity and neurodegenerative disorders, such as Alzheimer's disease. In plants, because of its importance in the assimilation and re-assimilat ... [truncated at 450 characters in length]|
|Author||Krajewski, Wojciech W; Collins, Ruairi; Holmberg-Schiavone, Lovisa; et al|
|Subject||Adenosine Triphosphate Amino Acid Sequence Animals Apoenzymes Binding Sites Catalytic Domain Cloning, Molecular Crystallography, X-Ray Dogs Drug Design Drug Interactions Glutamate-Ammonia Ligase Herbicides Humans Hydrogen Bonding Kinetics Ligands Magnesium Models, Chemical Models, Molecular Molecular Sequence Data Pharmaceutical Preparations Protein Binding Protein Conformation Protein Structure, Tertiary Sequence Homology, Amino Acid Substrate Specificity Temperature metabolism pharmacology chemistry chemistry genetics isolation and purification metabolism chemical synthesis chemistry metabolism pharmacology chemical synthesis chemistry|
Mechanism and substrate recognition of human holo ACP synthase.
|Abstract||Mammals utilize a single phosphopantetheinyl transferase for the posttranslational modification of at least three different apoproteins: the carrier protein components of cytosolic and mitochondrial fatty acid synthases and the aminoadipate semialdehyde reductase involved in lysine degradation. We determined the crystal structure of the human phosphopantetheinyl transferase, a eukaryotic phosphopantetheinyl transferase characterized, complexed wi ... [truncated at 450 characters in length]|
|Author||Bunkoczi, Gabor; Pasta, Saloni; Joshi, Anil; et al|
|Subject||Amino Acid Sequence Catalysis Coenzyme A Crystallography, X-Ray Fatty Acid Synthetase Complex Humans Kinetics Magnesium Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Protein Conformation Sequence Homology, Amino Acid Substrate Specificity metabolism chemistry genetics metabolism metabolism|