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Volumn 526, Issue 7572, 2015, Pages 277-280

Crystal structure of human glycine receptor-α3 bound to antagonist strychnine

Author keywords

[No Author keywords available]

Indexed keywords

GLYCINE RECEPTOR ALPHA 3; STRYCHNINE; UNCLASSIFIED DRUG; GLYCINE RECEPTOR; GLYCINE RECEPTOR ALPHA3 SUBUNIT;

EID: 84944052478     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature14972     Document Type: Article
Times cited : (194)

References (41)
  • 1
    • 41149168686 scopus 로고    scopus 로고
    • X-ray structure of a prokaryotic pentameric ligand-gated ion channel
    • Hilf, R. J. & Dutzler, R. X-ray structure of a prokaryotic pentameric ligand-gated ion channel. Nature 452, 375-379 (2008).
    • (2008) Nature , vol.452 , pp. 375-379
    • Hilf, R.J.1    Dutzler, R.2
  • 2
    • 58149242730 scopus 로고    scopus 로고
    • Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel
    • Hilf, R. J. & Dutzler, R. Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel. Nature 457, 115-118 (2009).
    • (2009) Nature , vol.457 , pp. 115-118
    • Hilf, R.J.1    Dutzler, R.2
  • 3
    • 58149267953 scopus 로고    scopus 로고
    • X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation
    • Bocquet, N. et al. X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation. Nature 457, 111-114 (2009).
    • (2009) Nature , vol.457 , pp. 111-114
    • Bocquet, N.1
  • 4
    • 84892910277 scopus 로고    scopus 로고
    • Crystal structures of a pentameric ligand-gated ion channel provide amechanismfor activation.Proc.NatlAcad
    • Sauguet, L. et al. Crystal structures of a pentameric ligand-gated ion channel provide amechanismfor activation.Proc.NatlAcad. Sci.USA111,966-971(2014).
    • (2014) Sci.USA , vol.111 , pp. 966-971
    • Sauguet, L.1
  • 5
    • 79957953215 scopus 로고    scopus 로고
    • Principles of activation and permeation in an anionselective Cys-loop receptor
    • Hibbs, R. E. & Gouaux, E. Principles of activation and permeation in an anionselective Cys-loop receptor. Nature 474, 54-60 (2011).
    • (2011) Nature , vol.474 , pp. 54-60
    • Hibbs, R.E.1    Gouaux, E.2
  • 6
    • 84905669878 scopus 로고    scopus 로고
    • Crystal structure of a human GABAA receptor
    • Miller, P. S. & Aricescu, A. R. Crystal structure of a human GABAA receptor. Nature 512, 270-275 (2014).
    • (2014) Nature , vol.512 , pp. 270-275
    • Miller, P.S.1    Aricescu, A.R.2
  • 7
    • 84906545550 scopus 로고    scopus 로고
    • X-ray structure of the mouse serotonin 5-HT3 receptor
    • Hassaine, G. et al. X-ray structure of the mouse serotonin 5-HT3 receptor. Nature 512, 276-281 (2014).
    • (2014) Nature , vol.512 , pp. 276-281
    • Hassaine, G.1
  • 8
    • 84906568725 scopus 로고    scopus 로고
    • X-ray structures of GluCl in apo states reveal a gating mechanism of Cys-loop receptors
    • Althoff, T., Hibbs, R. E., Banerjee, S. & Gouaux, E. X-ray structures of GluCl in apo states reveal a gating mechanism of Cys-loop receptors. Nature 512, 333-337 (2014).
    • (2014) Nature , vol.512 , pp. 333-337
    • Althoff, T.1    Hibbs, R.E.2    Banerjee, S.3    Gouaux, E.4
  • 9
    • 0034973097 scopus 로고    scopus 로고
    • The glycinergic inhibitory synapse
    • Legendre, P. The glycinergic inhibitory synapse. Cell. Mol. Life Sci. 58, 760-793 (2001).
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 760-793
    • Legendre, P.1
  • 10
    • 4644265039 scopus 로고    scopus 로고
    • Molecular structure and function of the glycine receptor chloride channel
    • Lynch, J. W. Molecular structure and function of the glycine receptor chloride channel. Physiol. Rev. 84, 1051-1095 (2004).
    • (2004) Physiol. Rev. , vol.84 , pp. 1051-1095
    • Lynch, J.W.1
  • 11
    • 30944455443 scopus 로고    scopus 로고
    • Glycine receptors: A new therapeutic target in pain pathways
    • Lynch, J. W. & Callister, R. J. Glycine receptors: A new therapeutic target in pain pathways. Curr. Opin. Investig. Drugs 7, 48-53 (2006).
    • (2006) Curr. Opin. Investig. Drugs , vol.7 , pp. 48-53
    • Lynch, J.W.1    Callister, R.J.2
  • 12
    • 84892181483 scopus 로고    scopus 로고
    • The impact of human hyperekplexia mutations on glycine receptor structure and function
    • Bode, A. & Lynch, J.W. The impact of human hyperekplexia mutations on glycine receptor structure and function. Mol. Brain 7, 2 (2014).
    • (2014) Mol. Brain , vol.7 , pp. 2
    • Bode, A.1    Lynch, J.W.2
  • 13
    • 0023225929 scopus 로고
    • Sequence and functional expression of the GABAA receptor shows a ligand-gated receptor super-family
    • Schofield, P. R. et al. Sequence and functional expression of the GABAA receptor shows a ligand-gated receptor super-family. Nature 328, 221-227 (1987).
    • (1987) Nature , vol.328 , pp. 221-227
    • Schofield, P.R.1
  • 14
    • 0001202076 scopus 로고
    • Conserved quaternary structure of ligandgated ion channels: The postsynaptic glycine receptor is a pentamer
    • Langosch, D., Thomas, L. & Betz, H. Conserved quaternary structure of ligandgated ion channels: The postsynaptic glycine receptor is a pentamer. Proc. Natl Acad. Sci. USA 85, 7394-7398 (1988).
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 7394-7398
    • Langosch, D.1    Thomas, L.2    Betz, H.3
  • 15
    • 0035902009 scopus 로고    scopus 로고
    • Crystal structure of an ACh-binding protein reveals the ligandbinding domain of nicotinic receptors
    • Brejc, K. et al. Crystal structure of an ACh-binding protein reveals the ligandbinding domain of nicotinic receptors. Nature 411, 269-276 (2001).
    • (2001) Nature , vol.411 , pp. 269-276
    • Brejc, K.1
  • 16
    • 1842475289 scopus 로고    scopus 로고
    • Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures
    • Celie, P. H. et al. Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures. Neuron 41, 907-914 (2004).
    • (2004) Neuron , vol.41 , pp. 907-914
    • Celie, P.H.1
  • 17
    • 27144473613 scopus 로고    scopus 로고
    • Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations
    • Hansen, S. B. et al. Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations. EMBO J. 24, 3635-3646 (2005).
    • (2005) EMBO J. , vol.24 , pp. 3635-3646
    • Hansen, S.B.1
  • 18
    • 84861866747 scopus 로고    scopus 로고
    • Molecular actions of smoking cessation drugs at a4b2 nicotinic receptors defined in crystal structures of a homologous binding protein
    • Billen, B. et al. Molecular actions of smoking cessation drugs at a4b2 nicotinic receptors defined in crystal structures of a homologous binding protein. Proc. Natl Acad. Sci. USA 109, 9173-9178 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 9173-9178
    • Billen, B.1
  • 19
    • 84930273363 scopus 로고    scopus 로고
    • Allosteric and hyperekplexicmutant phenotypes investigated on an a1 glycine receptor transmembrane structure
    • Moraga-Cid, G. et al. Allosteric and hyperekplexicmutant phenotypes investigated on an a1 glycine receptor transmembrane structure. Proc.Natl Acad. Sci. USA 112, 2865-2870 (2015).
    • (2015) Proc.Natl Acad. Sci. USA , vol.112 , pp. 2865-2870
    • Moraga-Cid, G.1
  • 21
    • 0036842245 scopus 로고    scopus 로고
    • Modulation of glycine receptor function: A novel approach for therapeutic intervention at inhibitory synapses?
    • Laube, B., Maksay, G., Schemm, R. & Betz, H. Modulation of glycine receptor function: A novel approach for therapeutic intervention at inhibitory synapses? Trends Pharmacol. Sci. 23, 519-527 (2002).
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 519-527
    • Laube, B.1    Maksay, G.2    Schemm, R.3    Betz, H.4
  • 22
    • 0025095280 scopus 로고
    • Alpha subunit variants of the human glycine receptor: Primary structures, functional expression and chromosomal localization of the corresponding genes
    • Grenningloh, G. et al. Alpha subunit variants of the human glycine receptor: primary structures, functional expression and chromosomal localization of the corresponding genes. EMBO J. 9, 771-776 (1990).
    • (1990) EMBO J. , vol.9 , pp. 771-776
    • Grenningloh, G.1
  • 23
    • 33744484568 scopus 로고    scopus 로고
    • Pharmacological characterisation of strychnine and brucine analogues at glycine and a7 nicotinic acetylcholine receptors
    • Jensen, A. A., Gharagozloo, P., Birdsall, N. J. & Zlotos, D. P. Pharmacological characterisation of strychnine and brucine analogues at glycine and a7 nicotinic acetylcholine receptors. Eur. J. Pharmacol. 539, 27-33 (2006).
    • (2006) Eur. J. Pharmacol. , vol.539 , pp. 27-33
    • Jensen, A.A.1    Gharagozloo, P.2    Birdsall, N.J.3    Zlotos, D.P.4
  • 24
    • 84906666443 scopus 로고    scopus 로고
    • Structure-activity relationships of strychnine analogs at glycine receptors
    • Mohsen, A. M., Heller, E., Holzgrabe, U., Jensen, A. A. & Zlotos, D. P. Structure-activity relationships of strychnine analogs at glycine receptors. Chem. Biodivers. 11, 1256-1262 (2014).
    • (2014) Chem. Biodivers. , vol.11 , pp. 1256-1262
    • Mohsen, A.M.1    Heller, E.2    Holzgrabe, U.3    Jensen, A.A.4    Zlotos, D.P.5
  • 25
    • 14644414132 scopus 로고    scopus 로고
    • The b subunit determines the ligand binding properties of synaptic glycine receptors
    • Grudzinska, J. et al. The b subunit determines the ligand binding properties of synaptic glycine receptors. Neuron 45, 727-739 (2005).
    • (2005) Neuron , vol.45 , pp. 727-739
    • Grudzinska, J.1
  • 26
    • 79953684899 scopus 로고    scopus 로고
    • A structural and mutagenic blueprint formolecular recognition of strychnine and d-tubocurarine by different Cys-loop receptors
    • Brams,M. et al. A structural and mutagenic blueprint formolecular recognition of strychnine and d-tubocurarine by different Cys-loop receptors. PLoS Biol. 9, e1001034 (2011).
    • (2011) PLoS Biol. , vol.9 , pp. e1001034
    • Brams, M.1
  • 27
    • 0024225307 scopus 로고
    • Glycine receptor heterogeneity in rat spinal cord during postnatal development
    • Becker, C. M., Hoch, W. & Betz, H. Glycine receptor heterogeneity in rat spinal cord during postnatal development. EMBO J. 7, 3717-3726 (1988).
    • (1988) EMBO J. , vol.7 , pp. 3717-3726
    • Becker, C.M.1    Hoch, W.2    Betz, H.3
  • 28
    • 0026536645 scopus 로고
    • Antagonism of ligand-gated ion channel receptors: Two domains of the glycine receptor a subunit form the strychnine-binding site
    • Vandenberg, R. J., French, C. R., Barry, P. H., Shine, J. & Schofield, P. R. Antagonism of ligand-gated ion channel receptors: Two domains of the glycine receptor a subunit form the strychnine-binding site. Proc. Natl Acad. Sci. USA 89, 1765-1769 (1992).
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 1765-1769
    • Vandenberg, R.J.1    French, C.R.2    Barry, P.H.3    Shine, J.4    Schofield, P.R.5
  • 29
    • 84885775931 scopus 로고    scopus 로고
    • A gating mechanism of pentameric ligand-gated ion channels
    • Calimet, N. et al. A gating mechanism of pentameric ligand-gated ion channels. Proc. Natl Acad. Sci. USA 110, E3987-E3996 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. E3987-E3996
    • Calimet, N.1
  • 30
    • 84907462413 scopus 로고    scopus 로고
    • Agonist and antagonist binding in human glycine receptors
    • Yu, R. et al. Agonist and antagonist binding in human glycine receptors. Biochemistry 53, 6041-6051 (2014).
    • (2014) Biochemistry , vol.53 , pp. 6041-6051
    • Yu, R.1
  • 31
    • 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
  • 32
    • 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
  • 33
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: A tool for high-throughput crystallography of protein-ligand complexes
    • Schuttelkopf, A. W. & van Aalten, D. M. PRODRG: A tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr. D 60, 1355-1363 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 1355-1363
    • Schuttelkopf, A.W.1    Van Aalten, D.M.2
  • 34
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A. & Dodson, E. J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53, 240-255 (1997).
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 35
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 36
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atomcontacts and structure validation for proteins and nucleic acids
    • Davis, I.W. et al. MolProbity: All-atomcontacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 35, W375-W383 (2007).
    • (2007) Nucleic Acids Res. , vol.35 , pp. W375-W383
    • Davis, I.W.1
  • 37
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: Application to microtubules and the ribosome
    • Baker, N. A., Sept, D., Joseph, S., Holst, M. J. & McCammon, J. A. Electrostatics of nanosystems: Application to microtubules and the ribosome. Proc. Natl Acad. Sci. USA 98, 10037-10041 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 10037-10041
    • Baker, N.A.1    Sept, D.2    Joseph, S.3    Holst, M.J.4    McCammon, J.A.5
  • 38
    • 0030404988 scopus 로고    scopus 로고
    • HOLE: A program for the analysis of the pore dimensions of ion channel structuralmodels
    • 376
    • Smart, O. S., Neduvelil, J. G., Wang, X., Wallace, B. A. & Sansom, M. S. HOLE: A program for the analysis of the pore dimensions of ion channel structuralmodels. J. Mol. Graph. 14, 354-360, 376 (1996).
    • (1996) J. Mol. Graph. , vol.14 , pp. 354-360
    • Smart, O.S.1    Neduvelil, J.G.2    Wang, X.3    Wallace, B.A.4    Sansom, M.S.5
  • 39
    • 33749641136 scopus 로고    scopus 로고
    • The PyMOL molecular graphics system
    • DeLano, W. L. The PyMOL molecular graphics system (DeLano Scientific, 2002).
    • (2002) DeLano Scientific
    • DeLano, W.L.1
  • 40
    • 36448991500 scopus 로고    scopus 로고
    • Clustal W and Clustal X version 2.0
    • Larkin, M. A. et al. Clustal W and Clustal X version 2.0. Bioinformatics 23, 2947-2948 (2007).
    • (2007) Bioinformatics , vol.23 , pp. 2947-2948
    • Larkin, M.A.1
  • 41
    • 1842785871 scopus 로고    scopus 로고
    • Functional characterisation of the humana1glycine receptor in a fluorescence-basedmembrane potential assay
    • Jensen, A. A.& Kristiansen,U. Functional characterisation of the humana1glycine receptor in a fluorescence-basedmembrane potential assay. Biochem. Pharmacol. 61, 1789-1799 (2004).
    • (2004) Biochem. Pharmacol. , vol.61 , pp. 1789-1799
    • Jensen, A.A.1    Kristiansen, U.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.