ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Ihre E-Mail wurde erfolgreich gesendet. Bitte prüfen Sie Ihren Maileingang.

Leider ist ein Fehler beim E-Mail-Versand aufgetreten. Bitte versuchen Sie es erneut.

Vorgang fortführen?

Exportieren
Filter
  • Hydrogen Bonding  (3)
  • Protein Structure, Secondary  (3)
  • 1
    facet.materialart.
    Unbekannt
    Hormone-dependent coactivator binding to a hydrophobic cleft on nuclear receptors (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1998-06-20
    Beschreibung: The ligand-binding domain of nuclear receptors contains a transcriptional activation function (AF-2) that mediates hormone-dependent binding of coactivator proteins. Scanning surface mutagenesis on the human thyroid hormone receptor was performed to define the site that binds the coactivators, glucocorticoid receptor-interacting protein 1 (GRIP1) and steroid receptor coactivator 1 (SRC-1). The residues involved encircle a small surface that contains a hydrophobic cleft. Ligand activation of transcription involves formation of this surface by folding the carboxyl-terminal alpha helix against a scaffold of three other helices. These features may represent general ones for nuclear receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feng, W -- Ribeiro, R C -- Wagner, R L -- Nguyen, H -- Apriletti, J W -- Fletterick, R J -- Baxter, J D -- Kushner, P J -- West, B L -- DK09516/DK/NIDDK NIH HHS/ -- DK51281/DK/NIDDK NIH HHS/ -- P41-RR01081/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1998 Jun 12;280(5370):1747-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Metabolic Research Unit, Box 0540, University of California San Francisco, San Francisco, CA 94143-0540, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9624051" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): HeLa Cells ; Histone Acetyltransferases ; Humans ; Ligands ; Models, Molecular ; Mutagenesis, Site-Directed ; Nuclear Receptor Coactivator 1 ; Nuclear Receptor Coactivator 2 ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Receptors, Retinoic Acid/metabolism ; Receptors, Thyroid Hormone/*chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Retinoid X Receptors ; Transcription Factors/*metabolism ; *Transcriptional Activation ; Triiodothyronine/*metabolism/pharmacology
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    AKTUELLE ARTIKEL
  • 2
    facet.materialart.
    Unbekannt
    A protein phosphorylation switch at the conserved allosteric site in GP (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1996-09-13
    Beschreibung: A phosphorylation-initiated mechanism of local protein refolding activates yeast glycogen phosphorylase (GP). Refolding of the phosphorylated amino-terminus was shown to create a hydrophobic cluster that wedges into the subunit interface of the enzyme to trigger activation. The phosphorylated threonine is buried in the allosteric site. The mechanism implicates glucose 6-phosphate, the allosteric inhibitor, in facilitating dephosphorylation by dislodging the buried covalent phosphate through binding competition. Thus, protein phosphorylation-dephosphorylation may also be controlled through regulation of the accessibility of the phosphorylation site to kinases and phosphatases. In mammalian glycogen phosphorylase, phosphorylation occurs at a distinct locus. The corresponding allosteric site binds a ligand activator, adenosine monophosphate, which triggers activation by a mechanism analogous to that of phosphorylation in the yeast enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, K -- Rath, V L -- Dai, S C -- Fletterick, R J -- Hwang, P K -- DK32822/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1996 Sep 13;273(5281):1539-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California at San Francisco, 513 Parnassus, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703213" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adenosine Monophosphate/metabolism ; Allosteric Site ; Amino Acid Sequence ; Animals ; Crystallography, X-Ray ; Enzyme Activation ; Enzyme Inhibitors/metabolism/pharmacology ; Glucose-6-Phosphate ; Glucosephosphates/metabolism/pharmacology ; Models, Molecular ; Molecular Sequence Data ; Phosphorylases/antagonists & inhibitors/*chemistry/*metabolism ; Phosphorylation ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Saccharomyces cerevisiae/enzymology
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    AKTUELLE ARTIKEL
  • 3
    facet.materialart.
    Unbekannt
    Locating the catalytic water molecule in serine proteases (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1993-07-30
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perona, J J -- Craik, C S -- Fletterick, R J -- DK-39304/DK/NIDDK NIH HHS/ -- GM13818-02/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Jul 30;261(5121):620-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8342029" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Catalysis ; Crystallization ; Hydrogen Bonding ; Protein Conformation ; Serine Endopeptidases/*chemistry ; Trypsin/chemistry ; Water/*analysis ; X-Ray Diffraction
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    AKTUELLE ARTIKEL
  • 4
    facet.materialart.
    Unbekannt
    Structural clues to prion replication (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1994-04-22
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, F E -- Pan, K M -- Huang, Z -- Baldwin, M -- Fletterick, R J -- Prusiner, S B -- New York, N.Y. -- Science. 1994 Apr 22;264(5158):530-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Francisco 94143-0518.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7909169" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Mice ; Mice, Transgenic ; Models, Biological ; Mutation ; PrPSc Proteins ; Prion Diseases/*metabolism/transmission ; Prions/*biosynthesis/chemistry/genetics/metabolism ; Protein Conformation ; Protein Structure, Secondary
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    AKTUELLE ARTIKEL
  • 5
    facet.materialart.
    Unbekannt
    Crystal structure of a catalytic antibody with a serine protease active site (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1994-08-19
    Beschreibung: The three-dimensional structure of an unusually active hydrolytic antibody with a phosphonate transition state analog (hapten) bound to the active site has been solved to 2.5 A resolution. The antibody (17E8) catalyzes the hydrolysis of norleucine and methionine phenyl esters and is selective for amino acid esters that have the natural alpha-carbon L configuration. A plot of the pH-dependence of the antibody-catalyzed reaction is bell-shaped with an activity maximum at pH 9.5; experiments on mechanism lend support to the formation of a covalent acyl-antibody intermediate. The structural and kinetic data are complementary and support a hydrolytic mechanism for the antibody that is remarkably similar to that of the serine proteases. The antibody active site contains a Ser-His dyad structure proximal to the phosphorous atom of the bound hapten that resembles two of the three components of the Ser-His-Asp catalytic triad of serine proteases. The antibody active site also contains a Lys residue to stabilize oxyanion formation, and a hydrophobic binding pocket for specific substrate recognition of norleucine and methionine side chains. The structure identifies active site residues that mediate catalysis and suggests specific mutations that may improve the catalytic efficiency of the antibody. This high resolution structure of a catalytic antibody-hapten complex shows that antibodies can converge on active site structures that have arisen through natural enzyme evolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, G W -- Guo, J -- Huang, W -- Fletterick, R J -- Scanlan, T S -- DK39304/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1994 Aug 19;265(5175):1059-64.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8066444" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Antibodies, Catalytic/*chemistry/immunology/metabolism ; Binding Sites ; Computer Graphics ; Crystallization ; Crystallography, X-Ray ; Haptens/metabolism ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Hydrolysis ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Serine Endopeptidases/*chemistry/metabolism
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    AKTUELLE ARTIKEL
  • 6
    facet.materialart.
    Unbekannt
    The three-dimensional structure of Asn102 mutant of trypsin: role of Asp102 in serine protease catalysis (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1987-08-21
    Beschreibung: The structure of the Asn102 mutant of trypsin was determined in order to distinguish whether the reduced activity of the mutant at neutral pH results from an altered active site conformation or from an inability to stabilize a positive charge on the active site histidine. The active site structure of the Asn102 mutant of trypsin is identical to the native enzyme with respect to the specificity pocket, the oxyanion hole, and the orientation of the nucleophilic serine. The observed decrease in rate results from the loss of nucleophilicity of the active site serine. This decreased nucleophilicity may result from stabilization of a His57 tautomer that is unable to accept the serine hydroxyl proton.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sprang, S -- Standing, T -- Fletterick, R J -- Stroud, R M -- Finer-Moore, J -- Xuong, N H -- Hamlin, R -- Rutter, W J -- Craik, C S -- AM26081/AM/NIADDK NIH HHS/ -- AM31507/AM/NIADDK NIH HHS/ -- GM24485/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Aug 21;237(4817):905-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3112942" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Asparagine ; Aspartic Acid ; Binding Sites ; Cattle ; Computer Simulation ; Crystallography ; Histidine ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Protein Conformation ; Rats ; Serine ; Structure-Activity Relationship ; *Trypsin
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    AKTUELLE ARTIKEL
Schließen ⊗
Diese Webseite nutzt Cookies und das Analyse-Tool Matomo. Weitere Informationen finden Sie hier...