메뉴 건너뛰기




Volumn 482, Issue 7386, 2012, Pages 547-551

Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BINDING PROTEIN; MUSCARINIC M2 RECEPTOR; QUINUCLIDINYL BENZILATE; TYROSINE;

EID: 84862777405     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature10753     Document Type: Article
Times cited : (671)

References (39)
  • 2
    • 0001536516 scopus 로고
    • The action of certain esters and ethers of choline, and their relation to muscarine
    • Dale, H. H. The action of certain esters and ethers of choline, and their relation to muscarine. J. Pharmacol. Exp. Ther. 6, 147-190 (1914).
    • (1914) J. Pharmacol. Exp. Ther. , vol.6 , pp. 147-190
    • Dale, H.H.1
  • 3
    • 0022367080 scopus 로고
    • Functional reconstitution of purified muscarinic receptors and inhibitory guanine nucleotide regulatory protein
    • Haga, K. et al. Functional reconstitution of purified muscarinic receptors and inhibitory guanine nucleotide regulatory protein. Nature 316, 731-733 (1985).
    • (1985) Nature , vol.316 , pp. 731-733
    • Haga, K.1
  • 4
    • 0022391964 scopus 로고
    • Purification of the muscarinic acetylcholine receptor from porcine brain
    • Haga, K. & Haga, T. Purification of the muscarinic acetylcholine receptor from porcine brain. J. Biol. Chem. 260, 7927-7935 (1985).
    • (1985) J. Biol. Chem. , vol.260 , pp. 7927-7935
    • Haga, K.1    Haga, T.2
  • 5
    • 0023040350 scopus 로고
    • Cloning, sequencing and expression of complementary DNA encoding the muscarinic acetylcholine receptor
    • Kubo, T. et al. Cloning, sequencing and expression of complementary DNA encoding the muscarinic acetylcholine receptor. Nature 323, 411-416 (1986).
    • (1986) Nature , vol.323 , pp. 411-416
    • Kubo, T.1
  • 6
    • 0022485749 scopus 로고
    • Cloning of the gene and cDNA for mammalian b-adrenergic receptor and homology with rhodopsin
    • Dixon, R. A. et al. Cloning of the gene and cDNA for mammalian b-adrenergic receptor and homology with rhodopsin. Nature 321, 75-79 (1986).
    • (1986) Nature , vol.321 , pp. 75-79
    • Dixon, R.A.1
  • 7
    • 0020373509 scopus 로고
    • Rhodopsin and bacteriorhodopsin: Structure-function relationships
    • Ovchinnikov, Y. A. Rhodopsin and bacteriorhodopsin: structure-function relationships. FEBS Lett. 148, 179-191 (1982).
    • (1982) FEBS Lett. , vol.148 , pp. 179-191
    • Ovchinnikov, Y.A.1
  • 8
    • 34548362105 scopus 로고    scopus 로고
    • Muscarinic acetylcholine receptors: Mutant mice provide new insights for drug development
    • Wess, J., Eglen, R. M. & Gautam, D. Muscarinic acetylcholine receptors: mutant mice provide new insights for drug development. Nature Rev. Drug Discov. 6, 721-733 (2007).
    • (2007) Nature Rev. Drug Discov. , vol.6 , pp. 721-733
    • Wess, J.1    Eglen, R.M.2    Gautam, D.3
  • 10
    • 0028079889 scopus 로고
    • Activation of a GTP-binding protein and a GTP-binding-protein-coupled receptor kinase (b-adrenergicreceptor kinase-1) by a muscarinic receptor M2 mutant lacking phosphorylation sites
    • Kameyama, K., Haga, K., Haga, T., Moro, O. & Sade, W. Activation of a GTP-binding protein and a GTP-binding-protein-coupled receptor kinase (b-adrenergicreceptor kinase-1) by a muscarinic receptor M2 mutant lacking phosphorylation sites. Eur. J. Biochem. FEBS 226, 267-276 (1994).
    • (1994) Eur. J. Biochem. FEBS , vol.226 , pp. 267-276
    • Kameyama, K.1    Haga, K.2    Haga, T.3    Moro, O.4    Sade, W.5
  • 11
    • 29344473088 scopus 로고    scopus 로고
    • The structure of the third intracellular loop of the muscarinic acetylcholine receptor M2 subtype
    • Ichiyama, S. et al. The structure of the third intracellular loop of the muscarinic acetylcholine receptor M2 subtype. FEBS Lett. 580, 23-26 (2006).
    • (2006) FEBS Lett. , vol.580 , pp. 23-26
    • Ichiyama, S.1
  • 12
    • 36448978229 scopus 로고    scopus 로고
    • GPCR engineering yields high-resolution structural insights into b2-adrenergic receptor function
    • Rosenbaum, D. M. et al. GPCR engineering yields high-resolution structural insights into b2-adrenergic receptor function. Science 318, 1266-1273 (2007).
    • (2007) Science , vol.318 , pp. 1266-1273
    • Rosenbaum, D.M.1
  • 13
    • 56749103466 scopus 로고    scopus 로고
    • The 2.6A? ngstrom crystal structure of a human A2A adenosine receptor bound to an antagonist
    • Jaakola, V. P. et al. The 2.6A? ngstrom crystal structure of a human A2A adenosine receptor bound to an antagonist. Science 322, 1211-1217 (2008).
    • (2008) Science , vol.322 , pp. 1211-1217
    • Jaakola, V.P.1
  • 14
    • 85027927015 scopus 로고    scopus 로고
    • Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists
    • Wu, B. et al. Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists. Science 330, 1066-1071 (2010).
    • (2010) Science , vol.330 , pp. 1066-1071
    • Wu, B.1
  • 15
    • 78449305788 scopus 로고    scopus 로고
    • Structure of the human dopamine D3 receptor in complex with a D2/D3 selective antagonist
    • Chien, E. Y. et al. Structure of the human dopamine D3 receptor in complex with a D2/D3 selective antagonist. Science 330, 1091-1095 (2010).
    • (2010) Science , vol.330 , pp. 1091-1095
    • Chien, E.Y.1
  • 16
    • 79960070651 scopus 로고    scopus 로고
    • Structure of the human histamine H1 receptor complex with doxepin
    • Shimamura, T. et al. Structure of the human histamine H1 receptor complex with doxepin. Nature 475, 65-70 (2011).
    • (2011) Nature , vol.475 , pp. 65-70
    • Shimamura, T.1
  • 17
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G protein-coupled receptor
    • Palczewski, K. et al. Crystal structure of rhodopsin: A G protein-coupled receptor. Science 289, 739-745 (2000).
    • (2000) Science , vol.289 , pp. 739-745
    • Palczewski, K.1
  • 18
    • 47949129742 scopus 로고    scopus 로고
    • Structure of a b1-adrenergic G-protein-coupled receptor
    • Warne, T. et al. Structure of a b1-adrenergic G-protein-coupled receptor. Nature 454, 486-491 (2008).
    • (2008) Nature , vol.454 , pp. 486-491
    • Warne, T.1
  • 19
    • 0041411237 scopus 로고    scopus 로고
    • Scanning mutagenesis studies of the M1 muscarinic acetylcholine receptor
    • Hulme, E. C., Lu, Z. L. & Bee, M. S. Scanning mutagenesis studies of the M1 muscarinic acetylcholine receptor. Receptors Channels 9, 215-228 (2003).
    • (2003) Receptors Channels , vol.9 , pp. 215-228
    • Hulme, E.C.1    Lu, Z.L.2    Bee, M.S.3
  • 20
    • 0032837005 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the putative human muscarinic M2 receptor binding site
    • Heitz, F. et al. Site-directed mutagenesis of the putative human muscarinic M2 receptor binding site. Eur. J. Pharmacol. 380, 183-195 (1999).
    • (1999) Eur. J. Pharmacol. , vol.380 , pp. 183-195
    • Heitz, F.1
  • 21
    • 0027496941 scopus 로고
    • Mutational analysis of muscarinic acetylcholine receptors: Structural basis of ligand/receptor/G protein interactions
    • Wess, J. Mutational analysis of muscarinic acetylcholine receptors: structural basis of ligand/receptor/G protein interactions. Life Sci. 53, 1447-1463 (1993).
    • (1993) Life Sci. , vol.53 , pp. 1447-1463
    • Wess, J.1
  • 22
    • 36349016730 scopus 로고    scopus 로고
    • Roof and floor of the muscarinic binding pocket: Variations in the bindingmodes of orthosteric ligands
    • Goodwin, J. A., Hulme, E. C., Langmead, C. J. & Tehan, B. G. Roof and floor of the muscarinic binding pocket: variations in the bindingmodes of orthosteric ligands. Mol. Pharmacol. 72, 1484-1496 (2007).
    • (2007) Mol. Pharmacol. , vol.72 , pp. 1484-1496
    • Goodwin, J.A.1    Hulme, E.C.2    Langmead, C.J.3    Tehan, B.G.4
  • 23
    • 0032756999 scopus 로고    scopus 로고
    • Alanine-scanning mutagenesis of transmembrane domain 6 of the M1 muscarinic acetylcholine receptor suggests that Tyr381 plays key roles in receptor function
    • Ward, S. D., Curtis, C. A. & Hulme, E. C. Alanine-scanning mutagenesis of transmembrane domain 6 of the M1 muscarinic acetylcholine receptor suggests that Tyr381 plays key roles in receptor function. Mol. Pharmacol. 56, 1031-1041 (1999).
    • (1999) Mol. Pharmacol. , vol.56 , pp. 1031-1041
    • Ward, S.D.1    Curtis, C.A.2    Hulme, E.C.3
  • 24
    • 0028291618 scopus 로고
    • Functional role in ligand binding and receptor activation of an asparagine residue present in the sixth transmembrane domain of all muscarinic acetylcholine receptors
    • Bluml, K., Mutschler, E. & Wess, J. Functional role in ligand binding and receptor activation of an asparagine residue present in the sixth transmembrane domain of all muscarinic acetylcholine receptors. J. Biol. Chem. 269, 18870-18876 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 18870-18876
    • Bluml, K.1    Mutschler, E.2    Wess, J.3
  • 25
    • 78651411166 scopus 로고    scopus 로고
    • Structure of a nanobody-stabilized active state of the b2 adrenoceptor
    • Rasmussen, S. G. et al. Structure of a nanobody-stabilized active state of the b2 adrenoceptor. Nature 469, 175-180 (2011).
    • (2011) Nature , vol.469 , pp. 175-180
    • Rasmussen, S.G.1
  • 26
    • 0036783718 scopus 로고    scopus 로고
    • Conformation of ligands bound to themuscarinic acetylcholine receptor
    • Furukawa, H. et al. Conformation of ligands bound to themuscarinic acetylcholine receptor. Mol. Pharmacol. 62, 778-787 (2002).
    • (2002) Mol. Pharmacol. , vol.62 , pp. 778-787
    • Furukawa, H.1
  • 27
    • 0036591656 scopus 로고    scopus 로고
    • Cation-p interactions in ligand recognition and catalysis
    • Zacharias, N. & Dougherty, D. A. Cation-p interactions in ligand recognition and catalysis. Trends Pharmacol. Sci. 23, 281-287 (2002).
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 281-287
    • Zacharias, N.1    Dougherty, D.A.2
  • 28
    • 79953017231 scopus 로고    scopus 로고
    • Crystal structures of a cysteine-modified mutant in loop D of acetylcholine-binding protein
    • Brams, M. et al. Crystal structures of a cysteine-modified mutant in loop D of acetylcholine-binding protein. J. Biol. Chem. 286, 4420-4428 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 4420-4428
    • Brams, M.1
  • 29
    • 57749122030 scopus 로고    scopus 로고
    • Crystal structures of the choline/acetylcholine substrate-binding protein ChoX from Sinorhizobium meliloti in the liganded and unliganded-closed states
    • Oswald, C. et al. Crystal structures of the choline/acetylcholine substrate-binding protein ChoX from Sinorhizobium meliloti in the liganded and unliganded-closed states. J. Biol. Chem. 283, 32848-32859 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 32848-32859
    • Oswald, C.1
  • 30
    • 33745550034 scopus 로고    scopus 로고
    • Structural insights into substrate traffic and inhibition in acetylcholinesterase
    • Colletier, J. P. et al. Structural insights into substrate traffic and inhibition in acetylcholinesterase. EMBO J. 25, 2746-2756 (2006).
    • (2006) EMBO J. , vol.25 , pp. 2746-2756
    • Colletier, J.P.1
  • 31
    • 79955033084 scopus 로고    scopus 로고
    • Evaluation of the Pichia pastoris expression system for the production of GPCRs for structural analysis
    • Asada, H. et al. Evaluation of the Pichia pastoris expression system for the production of GPCRs for structural analysis. Microb. Cell Fact. 10, 24 (2011).
    • (2011) Microb. Cell Fact. , vol.10 , pp. 24
    • Asada, H.1
  • 32
    • 0036417632 scopus 로고    scopus 로고
    • Optimisation of protein expression and establishment of the wave bioreactor for baculovirus/insect cell culture
    • Weber, W., Weber, E., Geisse, S. & Memmert, K. Optimisation of protein expression and establishment of the Wave Bioreactor for Baculovirus/insect cell culture. Cytotechnology 38, 77-85 (2002).
    • (2002) Cytotechnology , vol.38 , pp. 77-85
    • Weber, W.1    Weber, E.2    Geisse, S.3    Memmert, K.4
  • 33
    • 0021059388 scopus 로고
    • Affinity chromatography of the muscarinic acetylcholine receptor
    • Haga, K. & Haga, T. Affinity chromatography of the muscarinic acetylcholine receptor. J. Biol. Chem. 258, 13575-13579 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 13575-13579
    • Haga, K.1    Haga, T.2
  • 35
    • 67649392795 scopus 로고    scopus 로고
    • Crystallizing membrane proteins using lipidic mesophases
    • Caffrey, M. & Cherezov, V. Crystallizing membrane proteins using lipidic mesophases. Nature Protocols 4, 706-731 (2009).
    • (2009) Nature Protocols , vol.4 , pp. 706-731
    • Caffrey, M.1    Cherezov, V.2
  • 36
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 37
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy, A. J. Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr. D 63, 32-41 (2007).
    • (2007) Acta Crystallogr. D , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 38
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Cryst. 40, 658-674 (2007).
    • (2007) J. Appl. Cryst. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 39
    • 24644451703 scopus 로고    scopus 로고
    • A robust bulk-solvent correction and anisotropic scaling procedure
    • Afonine, P. V., Grosse-Kunstleve, R. W. & Adams, P. D. A robust bulk-solvent correction and anisotropic scaling procedure. Acta Crystallogr. D 61, 850-855 (2005).
    • (2005) Acta Crystallogr. D , vol.61 , pp. 850-855
    • Afonine, P.V.1    Grosse-Kunstleve, R.W.2    Adams, P.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.