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|
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|
Three-dimensional structure and enzymatic function of proapoptotic human p53-inducible quinone oxidoreductase PIG3.
|Abstract||Tumor suppressor p53 regulates the expression of p53-induced genes (PIG) that trigger apoptosis. PIG3 or TP53I3 is the only known member of the medium chain dehydrogenase/reductase superfamily induced by p53 and is used as a proapoptotic marker. Although the participation of PIG3 in the apoptotic pathway is proven, the protein and its mechanism of action were never characterized. We analyzed human PIG3 enzymatic function and found NADPH-dependent ... [truncated at 450 characters in length]|
|Author||Porté, Sergio; Valencia, Eva; Yakovtseva, Evgenia A; et al|
|Subject||Amino Acid Sequence Apoptosis Binding Sites Catalytic Domain Crystallography, X-Ray Humans Intracellular Signaling Peptides and Proteins Kinetics Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed NADP Phylogeny Protein Structure, Quaternary Proto-Oncogene Proteins Reactive Oxygen Species Recombinant Proteins Sequence Homology, Amino Acid Tumor Suppressor Protein p53 Tyrosine physiology genetics chemistry genetics metabolism metabolism chemistry genetics metabolism metabolism chemistry genetics metabolism metabolism chemistry|
Conformational stability and activity of p73 require a second helix in the tetramerization domain.
|Abstract||p73 and p63, the two ancestral members of the p53 family, are involved in neurogenesis, epithelial stem cell maintenance and quality control of female germ cells. The highly conserved oligomerization domain (OD) of tumor suppressor p53 is essential for its biological functions, and its structure was believed to be the prototype for all three proteins. However, we report that the ODs of p73 and p63 differ from the OD of p53 by containing an additi ... [truncated at 450 characters in length]|
|Author||Coutandin, D; Löhr, F; Niesen, F H; et al|
|Subject||Amino Acid Sequence Animals Conserved Sequence DNA-Binding Proteins Humans Mice Models, Molecular Molecular Sequence Data Mutation Nuclear Magnetic Resonance, Biomolecular Nuclear Proteins Phosphoproteins Protein Multimerization Protein Structure, Quaternary Protein Structure, Secondary Sequence Alignment Thermodynamics Trans-Activators Tumor Suppressor Protein p53 Tumor Suppressor Proteins chemistry genetics metabolism chemistry genetics metabolism chemistry metabolism chemistry metabolism chemistry metabolism chemistry genetics metabolism|
Crystal structures of human HMG-CoA synthase isoforms provide insights into inherited ketogenesis disorders and inhibitor design.
|Abstract||3-Hydroxy-3-methylglutaryl coenzyme A (CoA) synthase (HMGCS) catalyzes the condensation of acetyl-CoA and acetoacetyl-CoA into 3-hydroxy-3-methylglutaryl CoA. It is ubiquitous across the phylogenetic tree and is broadly classified into three classes. The prokaryotic isoform is essential in Gram-positive bacteria for isoprenoid synthesis via the mevalonate pathway. The eukaryotic cytosolic isoform also participates in the mevalonate pathway but it ... [truncated at 450 characters in length]|
|Author||Shafqat, Naeem; Turnbull, Andrew; Zschocke, Johannes; et al|
|Subject||Crystallography, X-Ray Dimerization Humans Hydroxymethylglutaryl-CoA Synthase Ketones Models, Molecular Mutation, Missense Protein Isoforms Protein Structure, Quaternary antagonists and inhibitors chemistry deficiency genetics metabolism antagonists and inhibitors chemistry deficiency genetics|