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Volumn 9, Issue 6, 2014, Pages

Crystallization scale preparation of a stable GPCR signaling complex between constitutively active rhodopsin and G-protein

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; HETEROTRIMERIC GUANINE NUCLEOTIDE BINDING PROTEIN; MEMBRANE PROTEIN; RHO FACTOR; RHODOPSIN; TRANSDUCIN; PROTEIN BINDING; PROTEIN SUBUNIT;

EID: 84903642406     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0098714     Document Type: Article
Times cited : (22)

References (53)
  • 1
    • 0038024615 scopus 로고    scopus 로고
    • The G-proteincoupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints
    • Fredriksson R, Lagerstrom MC, Lundin LG, Schioth HB (2003) The G-proteincoupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints. Mol Pharmacol 63: 1256-1272.
    • (2003) Mol Pharmacol , vol.63 , pp. 1256-1272
    • Fredriksson, R.1    Lagerstrom, M.C.2    Lundin, L.G.3    Schioth, H.B.4
  • 5
    • 38749131545 scopus 로고    scopus 로고
    • New G-protein-coupled receptor crystal structures: Insights and limitations
    • Kobilka B, Schertler GF (2008) New G-protein-coupled receptor crystal structures: insights and limitations. Trends Pharmacol Sci 29: 79-83.
    • (2008) Trends Pharmacol Sci , vol.29 , pp. 79-83
    • Kobilka, B.1    Schertler, G.F.2
  • 6
    • 84865436871 scopus 로고    scopus 로고
    • A crystal clear solution for determining G-protein-coupled receptor structures
    • Tate CG (2012) A crystal clear solution for determining G-protein-coupled receptor structures. Trends in Biochemical Sciences 37: 343-352.
    • (2012) Trends in Biochemical Sciences , vol.37 , pp. 343-352
    • Tate, C.G.1
  • 7
    • 84861984672 scopus 로고    scopus 로고
    • Fusion partner toolchest for the stabilization and crystallization of g protein-coupled receptors
    • Chun E, Thompson AA, Liu W, Roth CB, Griffith MT, et al. (2012) Fusion partner toolchest for the stabilization and crystallization of g protein-coupled receptors. Structure 20: 967-976.
    • (2012) Structure , vol.20 , pp. 967-976
    • Chun, E.1    Thompson, A.A.2    Liu, W.3    Roth, C.B.4    Griffith, M.T.5
  • 8
    • 84865138166 scopus 로고    scopus 로고
    • Membrane protein structure determination using crystallography and lipidic mesophases: Recent advances and successes
    • Caffrey M, Li D, Dukkipati A (2012) Membrane protein structure determination using crystallography and lipidic mesophases: recent advances and successes. Biochemistry 51: 6266-6288.
    • (2012) Biochemistry , vol.51 , pp. 6266-6288
    • Caffrey, M.1    Li, D.2    Dukkipati, A.3
  • 12
    • 79953242234 scopus 로고    scopus 로고
    • The structural basis of agonist-induced activation in constitutively active rhodopsin
    • Standfuss J, Edwards PC, D'Antona A, Fransen M, Xie G, et al. (2011) The structural basis of agonist-induced activation in constitutively active rhodopsin. Nature 471: 656-660.
    • (2011) Nature , vol.471 , pp. 656-660
    • Standfuss, J.1    Edwards, P.C.2    D'Antona, A.3    Fransen, M.4    Xie, G.5
  • 14
    • 84867840947 scopus 로고    scopus 로고
    • Structure of the agonist-bound neurotensin receptor
    • White JF, Noinaj N, Shibata Y, Love J, Kloss B, et al. (2012) Structure of the agonist-bound neurotensin receptor. Nature 490: 508-513.
    • (2012) Nature , vol.490 , pp. 508-513
    • White, J.F.1    Noinaj, N.2    Shibata, Y.3    Love, J.4    Kloss, B.5
  • 15
    • 84878582491 scopus 로고    scopus 로고
    • Insights into congenital stationary night blindness based on the structure of G90D rhodopsin
    • Singhal A, Ostermaier MK, Vishnivetskiy SA, Panneels V, Homan KT, et al. (2013) Insights into congenital stationary night blindness based on the structure of G90D rhodopsin. EMBO reports 14: 520-526.
    • (2013) EMBO Reports , vol.14 , pp. 520-526
    • Singhal, A.1    Ostermaier, M.K.2    Vishnivetskiy, S.A.3    Panneels, V.4    Homan, K.T.5
  • 16
    • 80051658642 scopus 로고    scopus 로고
    • Crystal structure of the beta2 adrenergic receptor-Gs protein complex
    • Rasmussen SG, DeVree BT, Zou Y, Kruse AC, Chung KY, et al. (2011) Crystal structure of the beta2 adrenergic receptor-Gs protein complex. Nature 477: 549-555.
    • (2011) Nature , vol.477 , pp. 549-555
    • Rasmussen, S.G.1    DeVree, B.T.2    Zou, Y.3    Kruse, A.C.4    Chung, K.Y.5
  • 18
    • 34447633368 scopus 로고    scopus 로고
    • Conformational complexity of G-protein-coupled receptors
    • Kobilka BK, Deupi X (2007) Conformational complexity of G-protein-coupled receptors. Trends Pharmacol Sci 28: 397-406.
    • (2007) Trends Pharmacol Sci , vol.28 , pp. 397-406
    • Kobilka, B.K.1    Deupi, X.2
  • 19
    • 0021646399 scopus 로고
    • The photocurrent, noise and spectral sensitivity of rods of the monkey Macaca fascicularis
    • Baylor DA, Nunn BJ, Schnapf JL (1984) The photocurrent, noise and spectral sensitivity of rods of the monkey Macaca fascicularis. The Journal of physiology 357: 575-607.
    • (1984) The Journal of Physiology , vol.357 , pp. 575-607
    • Baylor, D.A.1    Nunn, B.J.2    Schnapf, J.L.3
  • 20
    • 0343580431 scopus 로고    scopus 로고
    • A comparison of the efficiency of G protein activation by ligand-free and light-activated forms of rhodopsin
    • Melia TJ, Jr., Cowan CW, Angleson JK, Wensel TG (1997) A comparison of the efficiency of G protein activation by ligand-free and light-activated forms of rhodopsin. Biophysical journal 73: 3182-3191.
    • (1997) Biophysical Journal , vol.73 , pp. 3182-3191
    • Melia Jr., T.J.1    Cowan, C.W.2    Angleson, J.K.3    Wensel, T.G.4
  • 22
    • 0034100304 scopus 로고    scopus 로고
    • Assays for activation of recombinant expressed opsins by all-trans-retinals
    • Han M, Sakmar TP (2000) Assays for activation of recombinant expressed opsins by all-trans-retinals. Methods in enzymology 315: 251-267.
    • (2000) Methods in Enzymology , vol.315 , pp. 251-267
    • Han, M.1    Sakmar, T.P.2
  • 23
    • 0037465339 scopus 로고    scopus 로고
    • An opsin mutant with increased thermal stability
    • Xie G, Gross AK, Oprian DD (2003) An opsin mutant with increased thermal stability. Biochemistry 42: 1995-2001.
    • (2003) Biochemistry , vol.42 , pp. 1995-2001
    • Xie, G.1    Gross, A.K.2    Oprian, D.D.3
  • 25
    • 44649152217 scopus 로고    scopus 로고
    • Structural impact of the E113Q counterion mutation on the activation and deactivation pathways of the G protein-coupled receptor rhodopsin
    • Standfuss J, Zaitseva E, Mahalingam M, Vogel R (2008) Structural impact of the E113Q counterion mutation on the activation and deactivation pathways of the G protein-coupled receptor rhodopsin. J Mol Biol 380: 145-157.
    • (2008) J Mol Biol , vol.380 , pp. 145-157
    • Standfuss, J.1    Zaitseva, E.2    Mahalingam, M.3    Vogel, R.4
  • 26
    • 0032474444 scopus 로고    scopus 로고
    • Constitutive activation of opsin by mutation of methionine 257 on transmembrane helix 6
    • Han M, Smith SO, Sakmar TP (1998) Constitutive activation of opsin by mutation of methionine 257 on transmembrane helix 6. Biochemistry 37: 8253-8261.
    • (1998) Biochemistry , vol.37 , pp. 8253-8261
    • Han, M.1    Smith, S.O.2    Sakmar, T.P.3
  • 27
    • 81855226606 scopus 로고    scopus 로고
    • Preparation of an activated rhodopsin/transducin complex using a constitutively active mutant of rhodopsin
    • Xie G, D'Antona AM, Edwards PC, Fransen M, Standfuss J, et al. (2011) Preparation of an activated rhodopsin/transducin complex using a constitutively active mutant of rhodopsin. Biochemistry 50: 10399-10407.
    • (2011) Biochemistry , vol.50 , pp. 10399-10407
    • Xie, G.1    D'Antona, A.M.2    Edwards, P.C.3    Fransen, M.4    Standfuss, J.5
  • 29
    • 0028017506 scopus 로고
    • Identification of glutamic acid 113 as the Schiff base proton acceptor in the metarhodopsin II photointermediate of rhodopsin
    • Jager F, Fahmy K, Sakmar TP, Siebert F (1994) Identification of glutamic acid 113 as the Schiff base proton acceptor in the metarhodopsin II photointermediate of rhodopsin. Biochemistry 33: 10878-10882.
    • (1994) Biochemistry , vol.33 , pp. 10878-10882
    • Jager, F.1    Fahmy, K.2    Sakmar, T.P.3    Siebert, F.4
  • 31
    • 0001296931 scopus 로고
    • Interactions between photoexcited rhodopsin and light-activated enzymes in rods
    • Kühn H (1984) Interactions between photoexcited rhodopsin and light-activated enzymes in rods. Progress in retinal research 3: 123-156.
    • (1984) Progress in Retinal Research , vol.3 , pp. 123-156
    • Kühn, H.1
  • 32
    • 67049154294 scopus 로고    scopus 로고
    • Phospholipids are needed for the proper formation, stability, and function of the photoactivated rhodopsin-transducin complex
    • Jastrzebska B, Goc A, Golczak M, Palczewski K (2009) Phospholipids are needed for the proper formation, stability, and function of the photoactivated rhodopsin-transducin complex. Biochemistry 48: 5159-5170.
    • (2009) Biochemistry , vol.48 , pp. 5159-5170
    • Jastrzebska, B.1    Goc, A.2    Golczak, M.3    Palczewski, K.4
  • 33
    • 34547434085 scopus 로고    scopus 로고
    • Monomeric G protein-coupled receptor rhodopsin in solution activates its G protein transducin at the diffusion limit
    • Ernst OP, Gramse V, Kolbe M, Hofmann KP, Heck M (2007) Monomeric G protein-coupled receptor rhodopsin in solution activates its G protein transducin at the diffusion limit. Proc Natl Acad Sci U S A 104: 10859-10864.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 10859-10864
    • Ernst, O.P.1    Gramse, V.2    Kolbe, M.3    Hofmann, K.P.4    Heck, M.5
  • 34
    • 11144301981 scopus 로고    scopus 로고
    • The supramolecular structure of the GPCR rhodopsin in solution and native disc membranes
    • Suda K, Filipek S, Palczewski K, Engel A, Fotiadis D (2004) The supramolecular structure of the GPCR rhodopsin in solution and native disc membranes. Molecular membrane biology 21: 435-446.
    • (2004) Molecular Membrane Biology , vol.21 , pp. 435-446
    • Suda, K.1    Filipek, S.2    Palczewski, K.3    Engel, A.4    Fotiadis, D.5
  • 35
    • 0037426865 scopus 로고    scopus 로고
    • Atomicforce microscopy: Rhodopsin dimers in native disc membranes
    • Fotiadis D, Liang Y, Filipek S, Saperstein DA, Engel A, et al. (2003) Atomicforce microscopy: Rhodopsin dimers in native disc membranes. Nature 421: 127-128.
    • (2003) Nature , vol.421 , pp. 127-128
    • Fotiadis, D.1    Liang, Y.2    Filipek, S.3    Saperstein, D.A.4    Engel, A.5
  • 37
    • 84861079526 scopus 로고    scopus 로고
    • Conformational dynamics of activation for the pentameric complex of dimeric G protein-coupled receptor and heterotrimeric G protein
    • Orban T, Jastrzebska B, Gupta S, Wang B, Miyagi M, et al. (2012) Conformational dynamics of activation for the pentameric complex of dimeric G protein-coupled receptor and heterotrimeric G protein. Structure 20: 826-840.
    • (2012) Structure , vol.20 , pp. 826-840
    • Orban, T.1    Jastrzebska, B.2    Gupta, S.3    Wang, B.4    Miyagi, M.5
  • 39
    • 84892619091 scopus 로고    scopus 로고
    • Assembly of an activated rhodopsin-transducin complex in nanoscale lipid bilayers
    • D'Antona AM, Xie G, Sligar SG, Oprian DD (2014) Assembly of an activated rhodopsin-transducin complex in nanoscale lipid bilayers. Biochemistry 53: 127-134.
    • (2014) Biochemistry , vol.53 , pp. 127-134
    • D'Antona, A.M.1    Xie, G.2    Sligar, S.G.3    Oprian, D.D.4
  • 40
    • 34447509986 scopus 로고    scopus 로고
    • Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins
    • Bayburt TH, Leitz AJ, Xie G, Oprian DD, Sligar SG (2007) Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins. J Biol Chem 282: 14875-14881.
    • (2007) J Biol Chem , vol.282 , pp. 14875-14881
    • Bayburt, T.H.1    Leitz, A.J.2    Xie, G.3    Oprian, D.D.4    Sligar, S.G.5
  • 42
    • 0021268342 scopus 로고
    • Rhodopsinenhanced GTPase activity of the inhibitory GTP-binding protein of adenylate cyclase
    • Kanaho Y, Tsai SC, Adamik R, Hewlett EL, Moss J, et al. (1984) Rhodopsinenhanced GTPase activity of the inhibitory GTP-binding protein of adenylate cyclase. The Journal of biological chemistry 259: 7378-7381.
    • (1984) The Journal of Biological Chemistry , vol.259 , pp. 7378-7381
    • Kanaho, Y.1    Tsai, S.C.2    Adamik, R.3    Hewlett, E.L.4    Moss, J.5
  • 43
    • 84864853832 scopus 로고    scopus 로고
    • A fluorescence-detection size-exclusion chromatography-based thermostability assay for membrane protein precrystallization screening
    • Hattori M, Hibbs RE, Gouaux E (2012) A fluorescence-detection size-exclusion chromatography-based thermostability assay for membrane protein precrystallization screening. Structure 20: 1293-1299.
    • (2012) Structure , vol.20 , pp. 1293-1299
    • Hattori, M.1    Hibbs, R.E.2    Gouaux, E.3
  • 46
    • 80053141840 scopus 로고    scopus 로고
    • Structural flexibility of the G alpha s alpha-helical domain in the beta2-adrenoceptor Gs complex
    • Westfield GH, Rasmussen SG, Su M, Dutta S, DeVree BT, et al. (2011) Structural flexibility of the G alpha s alpha-helical domain in the beta2-adrenoceptor Gs complex. Proc Natl Acad Sci U S A 108: 16086-16091.
    • (2011) Proc Natl Acad Sci U S a , vol.108 , pp. 16086-16091
    • Westfield, G.H.1    Rasmussen, S.G.2    Su, M.3    Dutta, S.4    DeVree, B.T.5
  • 47
    • 84879093879 scopus 로고    scopus 로고
    • Conformational flexibility and structural dynamics in GPCR-mediated G protein activation: A perspective
    • Preininger AM, Meiler J, Hamm HE (2013) Conformational flexibility and structural dynamics in GPCR-mediated G protein activation: a perspective. Journal of Molecular Biology 425: 2288-2298.
    • (2013) Journal of Molecular Biology , vol.425 , pp. 2288-2298
    • Preininger, A.M.1    Meiler, J.2    Hamm, H.E.3
  • 48
    • 84889564886 scopus 로고    scopus 로고
    • Activation and allosteric modulation of a muscarinic acetylcholine receptor
    • Kruse AC, Ring AM, Manglik A, Hu J, Hu K, et al. (2013) Activation and allosteric modulation of a muscarinic acetylcholine receptor. Nature 504: 101-106.
    • (2013) Nature , vol.504 , pp. 101-106
    • Kruse, A.C.1    Ring, A.M.2    Manglik, A.3    Hu, J.4    Hu, K.5
  • 50
    • 80052083563 scopus 로고    scopus 로고
    • Nanobody stabilization of G protein-coupled receptor conformational states
    • Steyaert J, Kobilka BK (2011) Nanobody stabilization of G protein-coupled receptor conformational states. Current Opinion in Structural Biology 21: 567-572.
    • (2011) Current Opinion in Structural Biology , vol.21 , pp. 567-572
    • Steyaert, J.1    Kobilka, B.K.2
  • 51
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • Reeves PJ, Callewaert N, Contreras R, Khorana HG (2002) Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N- acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line. Proc Natl Acad Sci U S A 99: 13419-13424.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 52
    • 0023654299 scopus 로고
    • Allosteric behavior in transducin activation mediated by rhodopsin. Initial rate analysis of guanine nucleotide exchange
    • Wessling-Resnick M, Johnson GL (1987) Allosteric behavior in transducin activation mediated by rhodopsin. Initial rate analysis of guanine nucleotide exchange. The Journal of biological chemistry 262: 3697-3705.
    • (1987) The Journal of Biological Chemistry , vol.262 , pp. 3697-3705
    • Wessling-Resnick, M.1    Johnson, G.L.2


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