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|
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|
Structure of the human protein kinase MPSK1 reveals an atypical activation loop architecture.
|Abstract||The activation segment of protein kinases is structurally highly conserved and central to regulation of kinase activation. Here we report an atypical activation segment architecture in human MPSK1 comprising a beta sheet and a large alpha-helical insertion. Sequence comparisons suggested that similar activation segments exist in all members of the MPSK1 family and in MAST kinases. The consequence of this nonclassical activation segment on substra ... [truncated at 450 characters in length]|
|Author||Eswaran, Jeyanthy; Bernad, Antonio; Ligos, Jose M; et al|
|Subject||Amino Acid Sequence Animals Conserved Sequence Enzyme Activation Humans Kinetics Models, Molecular Molecular Sequence Data Protein Conformation Protein-Serine-Threonine Kinases Staurosporine Substrate Specificity Transcription Factors chemistry metabolism metabolism chemistry metabolism|
HD-PTP is a catalytically inactive tyrosine phosphatase due to a conserved divergence in its phosphatase domain.
|Abstract||The HD-PTP protein has been described as a tumor suppressor candidate and based on its amino acid sequence, categorized as a classical non-transmembrane protein tyrosine phosphatase (PTP). To date, no HD-PTP phosphorylated substrate has been identified and controversial results concerning its catalytic activity have been recently reported.|
|Author||Gingras, Marie-Claude; Zhang, Yu Ling; Kharitidi, Dmitri; et al|
|Subject||Amino Acid Sequence Catalysis Cell Line Conserved Sequence DNA, Complementary Humans Kinetics Protein Tyrosine Phosphatases, Non-Receptor Sequence Homology, Amino Acid chemistry genetics metabolism|
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|