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  • Articles  (67)
  • Mutation  (45)
  • Ligands  (25)
  • American Association for the Advancement of Science (AAAS)  (67)
  • American Chemical Society
  • American Institute of Physics (AIP)
  • Oxford University Press
  • Wiley
  • 1995-1999  (67)
  • 1980-1984
  • 1960-1964
  • 1999  (67)
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  • Articles  (67)
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  • American Association for the Advancement of Science (AAAS)  (67)
  • American Chemical Society
  • American Institute of Physics (AIP)
  • Oxford University Press
  • Wiley
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  • 1995-1999  (67)
  • 1980-1984
  • 1960-1964
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  • 1
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    Receptor for motilin identified in the human gastrointestinal system (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-06-26
    Description: Motilin is a 22-amino acid peptide hormone expressed throughout the gastrointestinal (GI) tract of humans and other species. It affects gastric motility by stimulating interdigestive antrum and duodenal contractions. A heterotrimeric guanosine triphosphate-binding protein (G protein)-coupled receptor for motilin was isolated from human stomach, and its amino acid sequence was found to be 52 percent identical to the human receptor for growth hormone secretagogues. The macrolide antibiotic erythromycin also interacted with the cloned motilin receptor, providing a molecular basis for its effects on the human GI tract. The motilin receptor is expressed in enteric neurons of the human duodenum and colon. Development of motilin receptor agonists and antagonists may be useful in the treatment of multiple disorders of GI motility.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feighner, S D -- Tan, C P -- McKee, K K -- Palyha, O C -- Hreniuk, D L -- Pong, S S -- Austin, C P -- Figueroa, D -- MacNeil, D -- Cascieri, M A -- Nargund, R -- Bakshi, R -- Abramovitz, M -- Stocco, R -- Kargman, S -- O'Neill, G -- Van Der Ploeg, L H -- Evans, J -- Patchett, A A -- Smith, R G -- Howard, A D -- New York, N.Y. -- Science. 1999 Jun 25;284(5423):2184-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Metabolic Disorders, Department of Medicinal Chemistry, Merck Research Laboratories, Building RY-80Y-265, 126 East Lincoln Avenue, Rahway, NJ 07065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10381885" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing ; Amino Acid Sequence ; Base Sequence ; Binding Sites ; Calcium/metabolism ; Cell Line ; Chromosome Mapping ; Chromosomes, Human, Pair 13 ; Cloning, Molecular ; Colon/*metabolism ; Erythromycin/metabolism ; GTP-Binding Proteins/metabolism ; Humans ; In Situ Hybridization ; Intestine, Small/*metabolism ; Ligands ; Molecular Sequence Data ; Motilin/analogs & derivatives/*metabolism ; Receptors, Gastrointestinal Hormone/*chemistry/*genetics/metabolism ; Receptors, Neuropeptide/*chemistry/*genetics/metabolism ; Stomach/*metabolism ; Thyroid Gland/metabolism ; Transfection
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  • 2
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    Requirement of yeast SGS1 and SRS2 genes for replication and transcription (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-22
    Description: The SGS1 gene of the yeast Saccharomyces cerevisiae encodes a DNA helicase with homology to the human Bloom's syndrome gene BLM and the Werner's syndrome gene WRN. The SRS2 gene of yeast also encodes a DNA helicase. Simultaneous deletion of SGS1 and SRS2 is lethal in yeast. Here, using a conditional mutation of SGS1, it is shown that DNA replication and RNA polymerase I transcription are drastically inhibited in the srs2Delta sgs1-ts strain at the restrictive temperature. Thus, SGS1 and SRS2 function in DNA replication and RNA polymerase I transcription. These functions may contribute to the various defects observed in Werner's and Bloom's syndromes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, S K -- Johnson, R E -- Yu, S L -- Prakash, L -- Prakash, S -- CA80882/CA/NCI NIH HHS/ -- GM19261/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Dec 17;286(5448):2339-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sealy Center for Molecular Science, University of Texas Medical Branch at Galveston, 6.104 Medical Research Building, 11th and Mechanic Streets, Galveston, TX 77555-1061, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10600744" target="_blank"〉PubMed〈/a〉
    Keywords: Bloom Syndrome/genetics ; Codon ; DNA Helicases/genetics/*physiology ; *DNA Replication ; DNA, Fungal/biosynthesis ; Fungal Proteins/genetics/*physiology ; Gene Deletion ; Genes, Fungal ; Humans ; Mutation ; RNA Polymerase I/metabolism ; RNA Polymerase II/metabolism ; RNA Polymerase III/metabolism ; RNA, Fungal/biosynthesis ; RNA, Messenger/biosynthesis/genetics ; RNA, Ribosomal/biosynthesis ; RNA, Transfer, Amino Acid-Specific/biosynthesis ; RecQ Helicases ; Saccharomyces cerevisiae/*genetics/metabolism ; *Saccharomyces cerevisiae Proteins ; *Transcription, Genetic ; Werner Syndrome/genetics
    Print ISSN: 0036-8075
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  • 3
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    Control of circadian rhythms and photoperiodic flowering by the Arabidopsis GIGANTEA gene (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-09-08
    Description: Photoperiodic responses in plants include flowering that is day-length-dependent. Mutations in the Arabidopsis thaliana GIGANTEA (GI) gene cause photoperiod-insensitive flowering and alteration of circadian rhythms. The GI gene encodes a protein containing six putative transmembrane domains. Circadian expression patterns of the GI gene and the clock-associated genes, LHY and CCA1, are altered in gi mutants, showing that GI is required for maintaining circadian amplitude and appropriate period length of these genes. The gi-1 mutation also affects light signaling to the clock, which suggests that GI participates in a feedback loop of the plant circadian system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Park, D H -- Somers, D E -- Kim, Y S -- Choy, Y H -- Lim, H K -- Soh, M S -- Kim, H J -- Kay, S A -- Nam, H G -- GM56006/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Sep 3;285(5433):1579-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Life Science, Pohang University of Science and Technology, Pohang, Kyungbuk, 790-784, Korea.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10477524" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*genetics/*physiology ; *Arabidopsis Proteins ; *Circadian Rhythm ; Cloning, Molecular ; Crosses, Genetic ; DNA-Binding Proteins/genetics ; Darkness ; Feedback ; Gene Expression Regulation, Plant ; *Genes, Plant ; Light ; Molecular Sequence Data ; Mutation ; Photoperiod ; Plant Leaves/physiology ; Plant Proteins/chemistry/*genetics/physiology ; Plant Structures/physiology ; Sequence Deletion ; Transcription Factors/genetics
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  • 4
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    Regulation of transcription by a protein methyltransferase (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-06-26
    Description: The p160 family of coactivators, SRC-1, GRIP1/TIF2, and p/CIP, mediate transcriptional activation by nuclear hormone receptors. Coactivator-associated arginine methyltransferase 1 (CARM1), a previously unidentified protein that binds to the carboxyl-terminal region of p160 coactivators, enhanced transcriptional activation by nuclear receptors, but only when GRIP1 or SRC-1a was coexpressed. Thus, CARM1 functions as a secondary coactivator through its association with p160 coactivators. CARM1 can methylate histone H3 in vitro, and a mutation in the putative S-adenosylmethionine binding domain of CARM1 substantially reduced both methyltransferase and coactivator activities. Thus, coactivator-mediated methylation of proteins in the transcription machinery may contribute to transcriptional regulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, D -- Ma, H -- Hong, H -- Koh, S S -- Huang, S M -- Schurter, B T -- Aswad, D W -- Stallcup, M R -- AG00093/AG/NIA NIH HHS/ -- DK43093/DK/NIDDK NIH HHS/ -- NS17269/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1999 Jun 25;284(5423):2174-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology HMR 301, University of Southern California, 2011 Zonal Avenue, Los Angeles, CA 90033, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10381882" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Histone Acetyltransferases ; Histones/metabolism ; Methylation ; Mice ; Molecular Sequence Data ; Mutation ; Nuclear Receptor Coactivator 1 ; Nuclear Receptor Coactivator 2 ; Nuclear Receptor Coactivator 3 ; Protein-Arginine N-Methyltransferases/chemistry/genetics/*metabolism ; Receptors, Androgen/metabolism ; Receptors, Estrogen/metabolism ; Receptors, Thyroid Hormone/metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Trans-Activators/*metabolism ; Transcription Factors/metabolism ; *Transcriptional Activation ; Transfection
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  • 5
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    Regulation of maternal behavior and offspring growth by paternally expressed Peg3 (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-04-09
    Description: Imprinted genes display parent-of-origin-dependent monoallelic expression that apparently regulates complex mammalian traits, including growth and behavior. The Peg3 gene is expressed in embryos and the adult brain from the paternal allele only. A mutation in the Peg3 gene resulted in growth retardation, as well as a striking impairment of maternal behavior that frequently resulted in death of the offspring. This result may be partly due to defective neuronal connectivity, as well as reduced oxytocin neurons in the hypothalamus, because mutant mothers were deficient in milk ejection. This study provides further insights on the evolution of epigenetic regulation of imprinted gene dosage in modulating mammalian growth and behavior.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, L -- Keverne, E B -- Aparicio, S A -- Ishino, F -- Barton, S C -- Surani, M A -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1999 Apr 9;284(5412):330-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome CRC Institute of Cancer and Developmental Biology, and Physiological Laboratory, University of Cambridge, Tennis Court Road, Cambridge CB2 1QR, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10195900" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; Brain/metabolism ; Crosses, Genetic ; Female ; Gene Expression ; Gene Targeting ; *Genomic Imprinting ; *Growth ; Hypothalamus/cytology/metabolism ; Kruppel-Like Transcription Factors ; Lactation ; Male ; *Maternal Behavior ; Mice ; Mutation ; Neural Pathways ; Neurons/metabolism ; Oxytocin/metabolism ; Phenotype ; *Protein Kinases ; Proteins/genetics/*physiology ; *Transcription Factors ; *Weight Gain
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  • 6
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    Bile acids: natural ligands for an orphan nuclear receptor (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-05-21
    Description: Bile acids regulate the transcription of genes that control cholesterol homeostasis through molecular mechanisms that are poorly understood. Physiological concentrations of free and conjugated chenodeoxycholic acid, lithocholic acid, and deoxycholic acid activated the farnesoid X receptor (FXR; NR1H4), an orphan nuclear receptor. As ligands, these bile acids and their conjugates modulated interaction of FXR with a peptide derived from steroid receptor coactivator 1. These results provide evidence for a nuclear bile acid signaling pathway that may regulate cholesterol homeostasis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parks, D J -- Blanchard, S G -- Bledsoe, R K -- Chandra, G -- Consler, T G -- Kliewer, S A -- Stimmel, J B -- Willson, T M -- Zavacki, A M -- Moore, D D -- Lehmann, J M -- F32 DK09793/DK/NIDDK NIH HHS/ -- R01 DK53366/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1999 May 21;284(5418):1365-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biochemistry, Glaxo Wellcome Research and Development, Research Triangle Park NC, 27709, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10334993" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bile Acids and Salts/chemistry/*metabolism/pharmacology ; Carrier Proteins/metabolism ; Cell Line ; Chenodeoxycholic Acid/*metabolism/pharmacology ; Cholesterol/metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Deoxycholic Acid/metabolism/pharmacology ; Histone Acetyltransferases ; Homeostasis ; Humans ; Ligands ; Lithocholic Acid/metabolism/pharmacology ; Mice ; Nuclear Receptor Coactivator 1 ; *Organic Anion Transporters, Sodium-Dependent ; Protein Conformation ; Receptors, Cytoplasmic and Nuclear/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Structure-Activity Relationship ; *Symporters ; Transcription Factors/chemistry/genetics/*metabolism ; Transfection
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  • 7
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    Apaf-1 and caspase-9 in p53-dependent apoptosis and tumor inhibition (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-04-02
    Description: The ability of p53 to promote apoptosis in response to mitogenic oncogenes appears to be critical for its tumor suppressor function. Caspase-9 and its cofactor Apaf-1 were found to be essential downstream components of p53 in Myc-induced apoptosis. Like p53 null cells, mouse embryo fibroblast cells deficient in Apaf-1 and caspase-9, and expressing c-Myc, were resistant to apoptotic stimuli that mimic conditions in developing tumors. Inactivation of Apaf-1 or caspase-9 substituted for p53 loss in promoting the oncogenic transformation of Myc-expressing cells. These results imply a role for Apaf-1 and caspase-9 in controlling tumor development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Soengas, M S -- Alarcon, R M -- Yoshida, H -- Giaccia, A J -- Hakem, R -- Mak, T W -- Lowe, S W -- CA13106/CA/NCI NIH HHS/ -- CA64489/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1999 Apr 2;284(5411):156-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10102818" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Apoptotic Protease-Activating Factor 1 ; Caspase 9 ; Caspases/genetics/*physiology ; Cell Division ; Cell Transformation, Neoplastic ; Cells, Cultured ; Cytochrome c Group/metabolism ; Genes, myc ; *Genes, p53 ; Genes, ras ; Mice ; Mice, Nude ; Mitochondria/metabolism ; Mutation ; Neoplasms, Experimental/genetics/metabolism/*pathology ; Proteins/genetics/*physiology ; Tumor Suppressor Protein p53/metabolism
    Print ISSN: 0036-8075
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  • 8
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    An allele of COL9A2 associated with intervertebral disc disease (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-07-20
    Description: Intervertebral disc disease is one of the most common musculoskeletal disorders. A number of environmental and anthropometric risk factors may contribute to it, and recent reports have suggested the importance of genetic factors as well. The COL9A2 gene, which codes for one of the polypeptide chains of collagen IX that is expressed in the intervertebral disc, was screened for sequence variations in individuals with intervertebral disc disease. The analysis identified a putative disease-causing sequence variation that converted a codon for glutamine to one for tryptophan in six out of the 157 individuals but in none of 174 controls. The tryptophan allele cosegregated with the disease phenotype in the four families studied, giving a lod score (logarithm of odds ratio) for linkage of 4.5, and subsequent linkage disequilibrium analysis conditional on linkage gave an additional lod score of 7.1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Annunen, S -- Paassilta, P -- Lohiniva, J -- Perala, M -- Pihlajamaa, T -- Karppinen, J -- Tervonen, O -- Kroger, H -- Lahde, S -- Vanharanta, H -- Ryhanen, L -- Goring, H H -- Ott, J -- Prockop, D J -- Ala-Kokko, L -- AR39740/AR/NIAMS NIH HHS/ -- HG00008/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1999 Jul 16;285(5426):409-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Collagen Research Unit, Biocenter and Department of Medical Biochemistry, University of Oulu, 90220 Oulu, Finland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10411504" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Alleles ; Amino Acid Substitution ; Case-Control Studies ; Codon ; Collagen/chemistry/*genetics ; *Collagen Type IX ; Female ; Genetic Linkage ; *Genetic Predisposition to Disease ; Humans ; Intervertebral Disc Displacement/*genetics ; Linkage Disequilibrium ; Male ; Middle Aged ; Mutation ; Penetrance ; Polymorphism, Genetic ; Sciatica/*genetics ; Tryptophan/genetics
    Print ISSN: 0036-8075
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  • 9
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    Mouse models of tumor development in neurofibromatosis type 1 (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-11
    Description: Neurofibromatosis type 1 (NF1) is a prevalent familial cancer syndrome resulting from germ line mutations in the NF1 tumor suppressor gene. Hallmark features of the disease are the development of benign peripheral nerve sheath tumors (neurofibromas), which can progress to malignancy. Unlike humans, mice that are heterozygous for a mutation in Nf1 do not develop neurofibromas. However, as described here, chimeric mice composed in part of Nf1-/- cells do, which demonstrates that loss of the wild-type Nf1 allele is rate-limiting in tumor formation. In addition, mice that carry linked germ line mutations in Nf1 and p53 develop malignant peripheral nerve sheath tumors (MPNSTs), which supports a cooperative and causal role for p53 mutations in MPNST development. These two mouse models provide the means to address fundamental aspects of disease development and to test therapeutic strategies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cichowski, K -- Shih, T S -- Schmitt, E -- Santiago, S -- Reilly, K -- McLaughlin, M E -- Bronson, R T -- Jacks, T -- New York, N.Y. -- Science. 1999 Dec 10;286(5447):2172-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology and Center for Cancer Research and Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10591652" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Chimera ; *Disease Models, Animal ; Female ; *Genes, Neurofibromatosis 1 ; Genes, p53 ; Germ-Line Mutation ; Humans ; Loss of Heterozygosity ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Mutation ; Nerve Sheath Neoplasms/*genetics/*pathology ; Nerve Tissue Proteins/analysis/physiology ; Neurofibromatosis 1/*genetics/*pathology ; Neurofibromin 1 ; Proteins/analysis/physiology ; S100 Proteins/analysis ; Schwann Cells/chemistry/ultrastructure ; Stem Cells
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  • 10
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    Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-04-30
    Description: The PDZ protein interaction domain of neuronal nitric oxide synthase (nNOS) can heterodimerize with the PDZ domains of postsynaptic density protein 95 and syntrophin through interactions that are not mediated by recognition of a typical carboxyl-terminal motif. The nNOS-syntrophin PDZ complex structure revealed that the domains interact in an unusual linear head-to-tail arrangement. The nNOS PDZ domain has two opposite interaction surfaces-one face has the canonical peptide binding groove, whereas the other has a beta-hairpin "finger." This nNOS beta finger docks in the syntrophin peptide binding groove, mimicking a peptide ligand, except that a sharp beta turn replaces the normally required carboxyl terminus. This structure explains how PDZ domains can participate in diverse interaction modes to assemble protein networks.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hillier, B J -- Christopherson, K S -- Prehoda, K E -- Bredt, D S -- Lim, W A -- New York, N.Y. -- Science. 1999 Apr 30;284(5415):812-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10221915" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Crystallography, X-Ray ; Dimerization ; *Dystrophin-Associated Proteins ; Ligands ; Membrane Proteins/*chemistry/metabolism ; Molecular Sequence Data ; Muscle Proteins/*chemistry/metabolism ; Nitric Oxide Synthase/*chemistry/metabolism ; Nitric Oxide Synthase Type I ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Signal Transduction
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