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  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-06-04
    Description: Forty years ago, a simple model of allosteric mechanisms (indirect interactions between distinct sites), used initially to explain feedback-inhibited enzymes, was presented by Monod, Wyman, and Changeux. We review the MWC theory and its applications for the understanding of signal transduction in biology, and also identify remaining issues that deserve theoretical and experimental substantiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Changeux, Jean-Pierre -- Edelstein, Stuart J -- New York, N.Y. -- Science. 2005 Jun 3;308(5727):1424-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Receptors and Cognition, Institut Pasteur, 75724 Paris Cedex 15, France. changeux@pasteur.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15933191" target="_blank"〉PubMed〈/a〉
    Keywords: *Allosteric Regulation ; Binding Sites ; Enzymes/metabolism ; Ligands ; Models, Biological ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Receptors, Cell Surface/physiology ; Signal Transduction/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 2011-01-21
    Description: General anaesthetics have enjoyed long and widespread use but their molecular mechanism of action remains poorly understood. There is good evidence that their principal targets are pentameric ligand-gated ion channels (pLGICs) such as inhibitory GABA(A) (gamma-aminobutyric acid) receptors and excitatory nicotinic acetylcholine receptors, which are respectively potentiated and inhibited by general anaesthetics. The bacterial homologue from Gloeobacter violaceus (GLIC), whose X-ray structure was recently solved, is also sensitive to clinical concentrations of general anaesthetics. Here we describe the crystal structures of the complexes propofol/GLIC and desflurane/GLIC. These reveal a common general-anaesthetic binding site, which pre-exists in the apo-structure in the upper part of the transmembrane domain of each protomer. Both molecules establish van der Waals interactions with the protein; propofol binds at the entrance of the cavity whereas the smaller, more flexible, desflurane binds deeper inside. Mutations of some amino acids lining the binding site profoundly alter the ionic response of GLIC to protons, and affect its general-anaesthetic pharmacology. Molecular dynamics simulations, performed on the wild type (WT) and two GLIC mutants, highlight differences in mobility of propofol in its binding site and help to explain these effects. These data provide a novel structural framework for the design of general anaesthetics and of allosteric modulators of brain pLGICs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nury, Hugues -- Van Renterghem, Catherine -- Weng, Yun -- Tran, Alphonso -- Baaden, Marc -- Dufresne, Virginie -- Changeux, Jean-Pierre -- Sonner, James M -- Delarue, Marc -- Corringer, Pierre-Jean -- R01 GM069379/GM/NIGMS NIH HHS/ -- England -- Nature. 2011 Jan 20;469(7330):428-31. doi: 10.1038/nature09647.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut Pasteur, Groupe Recepteurs-Canaux, F-75015 Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21248852" target="_blank"〉PubMed〈/a〉
    Keywords: Anesthetics, General/*chemistry/*metabolism ; Binding Sites/genetics ; Crystallography, X-Ray ; Cyanobacteria/*chemistry ; Electrophysiological Phenomena ; Isoflurane/*analogs & derivatives/chemistry/metabolism ; Ligand-Gated Ion Channels/*chemistry/genetics/*metabolism ; Ligands ; Models, Molecular ; Molecular Dynamics Simulation ; Mutant Proteins/chemistry/genetics/metabolism ; Propofol/*chemistry/metabolism ; Protein Binding ; Protein Structure, Tertiary ; Protons
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 2010-02-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vasbinder, Jan W -- Andersson, Bertil -- Arthur, W Brian -- Boasson, Maarten -- de Boer, Rob -- Changeux, Jean Pierre -- Domingo, Esteban -- Eigen, Manfred -- Fersht, Alan -- Frenkel, Daan -- Rees, Martin -- Groen, Theo -- Huber, Robert -- Hunt, Tim -- Holland, John -- May, Robert -- Norrby, Erling -- Nijkamp, Peter -- Lehn, Jean Marie -- Rabbinge, Rudy -- Scheffer, Marten -- Schuster, Peter -- Serageldin, Ismail -- Stuip, Jan -- de Vries, Jan -- van Vierssen, Wim -- Willems, Rein -- England -- Nature. 2010 Feb 18;463(7283):876. doi: 10.1038/463876a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20164899" target="_blank"〉PubMed〈/a〉
    Keywords: Academies and Institutes/*economics/trends ; Conservation of Natural Resources/economics/trends ; European Union ; Humans ; Internationality ; Netherlands ; Research/*economics/trends ; *Research Design
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 4
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-09-21
    Description: The nicotine receptor for the neurotransmitter acetylcholine is an allosteric protein composed of four different subunits assembled in a transmembrane pentamer alpha 2 beta gamma delta. The protein carries two acetylcholine sites at the level of the alpha subunits and contains the ion channel. The complete sequence of the four subunits is known. The membrane-bound protein undergoes conformational transitions that regulate the opening of the ion channel and are affected by various categories of pharmacologically active ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Changeux, J P -- Devillers-Thiery, A -- Chemouilli, P -- New York, N.Y. -- Science. 1984 Sep 21;225(4668):1335-45.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6382611" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Amino Acid Sequence ; Animals ; Binding Sites ; Cell Membrane/ultrastructure ; Cloning, Molecular ; DNA/analysis ; Electric Organ/metabolism ; Electrophorus ; Macromolecular Substances ; Protein Conformation ; *Receptors, Nicotinic/genetics/metabolism ; Torpedo
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 1986-11-14
    Description: The chromosomal localization of the genes encoding the four subunits of muscle nicotinic receptor was determined by analyzing restriction fragment length polymorphisms between two mouse species Mus musculus domesticus (DBA/2) and Mus spretus (SPE). Analysis of the progeny of the interspecies mouse backcross (DBA/2 X SPE) X DBA/2 showed that the alpha-subunit gene cosegregates with the alpha-cardiac actin gene on chromosome 17, that the beta-subunit gene is located on chromosome 11, and that the gamma- and delta-subunit genes cosegregate and are located on chromosome 1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heidmann, O -- Buonanno, A -- Geoffroy, B -- Robert, B -- Guenet, J L -- Merlie, J P -- Changeux, J P -- New York, N.Y. -- Science. 1986 Nov 14;234(4778):866-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3022377" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/genetics ; Animals ; *Chromosome Mapping ; Crosses, Genetic ; DNA/genetics ; DNA Restriction Enzymes ; Mice ; Mice, Inbred DBA ; Muridae ; Muscles/*analysis ; Nucleic Acid Hybridization ; Polymorphism, Genetic ; Receptors, Nicotinic/*genetics ; Species Specificity
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
    Publication Date: 1992-08-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Epstein, H F -- Fischman, D A -- Bader, D -- Changeux, J P -- Buckhold, K -- Ordahl, C P -- Hoffman, E -- Kedes, L H -- Konieczny, S -- Leinwand, L A -- New York, N.Y. -- Science. 1992 Aug 7;257(5071):738.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1496388" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Child ; Humans ; Male ; Muscles/*transplantation ; Muscular Dystrophies/*surgery ; Transplantation/adverse effects
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
    Publication Date: 2008-11-07
    Description: Pentameric ligand-gated ion channels from the Cys-loop family mediate fast chemo-electrical transduction, but the mechanisms of ion permeation and gating of these membrane proteins remain elusive. Here we present the X-ray structure at 2.9 A resolution of the bacterial Gloeobacter violaceus pentameric ligand-gated ion channel homologue (GLIC) at pH 4.6 in an apparently open conformation. This cationic channel is known to be permanently activated by protons. The structure is arranged as a funnel-shaped transmembrane pore widely open on the outer side and lined by hydrophobic residues. On the inner side, a 5 A constriction matches with rings of hydrophilic residues that are likely to contribute to the ionic selectivity. Structural comparison with ELIC, a bacterial homologue from Erwinia chrysanthemi solved in a presumed closed conformation, shows a wider pore where the narrow hydrophobic constriction found in ELIC is removed. Comparative analysis of GLIC and ELIC reveals, in concert, a rotation of each extracellular beta-sandwich domain as a rigid body, interface rearrangements, and a reorganization of the transmembrane domain, involving a tilt of the M2 and M3 alpha-helices away from the pore axis. These data are consistent with a model of pore opening based on both quaternary twist and tertiary deformation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bocquet, Nicolas -- Nury, Hugues -- Baaden, Marc -- Le Poupon, Chantal -- Changeux, Jean-Pierre -- Delarue, Marc -- Corringer, Pierre-Jean -- England -- Nature. 2009 Jan 1;457(7225):111-4. doi: 10.1038/nature07462. Epub 2008 Nov 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pasteur Institute, G5 Group of Channel-Receptor, CNRS URA 2182.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18987633" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallography, X-Ray ; Cyanobacteria/*chemistry ; Hydrophobic and Hydrophilic Interactions ; *Ion Channel Gating ; Ion Channels/*chemistry/*metabolism ; Ligands ; Models, Molecular ; Pectobacterium chrysanthemi/chemistry ; Protein Structure, Quaternary ; Protein Subunits/chemistry/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 8
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Current Opinion in Structural Biology 4 (1994), S. 554-565 
    ISSN: 0959-440X
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1420-9071
    Keywords: Allosteric proteins ; MWC model ; ligand-gated channels ; neuronal nicotinic acetylcholine receptors ; stochastic models
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract A key statement of the 1965 Monod-Wyman-Changeux (MWC) model for allosteric proteins concerns the distinction between the ligand-binding function ( $$\bar Y$$ ) and the relevant state function ( $$\bar R$$ ). Sequential models predict overlapping behavior of the two functions. In contrast, a straightforward experimental consequence of the MWC model is that for an oligomeric protein the parameters which characterize the two functions should differ significantly. Two situations, where $$\bar R 〉 \bar Y$$ and the system ishyper-responsive or where $$\bar R〈 \bar Y$$ and the system ishypo-responsive, have been encountered. Indeed, the hyper-responsive pattern was first observed for the enzyme aspartate transcarbamoylase, by comparing $$\bar Y$$ with $$\bar R$$ monitored by a change in sedimentation. Extensions of the theory to ligand-gated channels led to the suggestion that, on the one hand, hyper-responsive properties also occur with high-affinity mutants. On the other hand, native channels of the acetylcholine neuronalα7 receptor and low-affinity mutants of the glycine receptor can be interpreted in terms of the hypo-responsive pattern. For the ligand-gated channels, whereas $$\bar R$$ is detected directly by ion flux, ligand binding has rarely been measured and the formation of desensitized states may complicate the analysis. However, stochastic models incorporating both binding and channel opening for single molecules predict differences that should be measurable with new experimental approaches, particularly fluorescence correlation spectroscopy.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 0012-1606
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
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