메뉴 건너뛰기




Volumn 28, Issue 10, 2012, Pages 837-844

Handling G-protein-coupled receptors: Expression, purification and in vitro stabilization;Manipulation des récepteurs couplés aux protéines G Expression, purification et stabilisation in vitro

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; RECOMBINANT PROTEIN;

EID: 84867693733     PISSN: 07670974     EISSN: 19585381     Source Type: Journal    
DOI: 10.1051/medsci/20122810011     Document Type: Review
Times cited : (7)

References (41)
  • 1
    • 48849110480 scopus 로고    scopus 로고
    • Automated large-scale purification of a recombinant g protein-coupled neurotensin receptor
    • chapter 6 : Unit 6.8
    • White JF, Grisshammer R. Automated large-scale purification of a recombinant G protein-coupled neurotensin receptor. Curr Protoc Protein Sci 2007; chapter 6 : Unit 6.8.
    • (2007) Curr Protoc Protein Sci
    • White, J.F.1    Grisshammer, R.2
  • 2
    • 77949892910 scopus 로고    scopus 로고
    • Leukotriene blt2 receptor monomers activate the gi2 gtp-binding protein more efficiently than dimers
    • Arcemisbéhère L, Sen T, Boudier L, et al. Leukotriene BLT2 receptor monomers activate the Gi2 GTP-binding protein more efficiently than dimers. J Biol Chem 2010 ; 285 : 6337-47.
    • (2010) J Biol Chem , vol.285 , pp. 6337-47
    • Arcemisbéhère, L.1    Sen, T.2    Boudier, L.3
  • 4
    • 77954279046 scopus 로고    scopus 로고
    • Structure of a gpcr ligand in its receptor-bound state: Leukotriene b4 adopts a highly constrained conformation when associated to human blt2
    • Catoire L, Damian M, Giusti F, et al. Structure of a GPCR ligand in its receptor-bound state: leukotriene B4 adopts a highly constrained conformation when associated to human BLT2. J Am Chem Soc 2010 ; 132 : 9049-57.
    • (2010) J Am Chem Soc , vol.132 , pp. 9049-57
    • Catoire, L.1    Damian, M.2    Giusti, F.3
  • 5
    • 32944474906 scopus 로고    scopus 로고
    • Solubilization, purification and mass spectrometry analysis of the human -opioid receptor expressed in pichia pastoris
    • Sarramegna V, Muller I, Mousseau G, et al. Solubilization, purification and mass spectrometry analysis of the human -opioid receptor expressed in Pichia pastoris. Protein Expr Purif 2005 ; 43 : 85-93.
    • (2005) Protein Expr Purif , vol.43 , pp. 85-93
    • Sarramegna, V.1    Muller, I.2    Mousseau, G.3
  • 6
    • 79960070651 scopus 로고    scopus 로고
    • Structure of the human histamine h1 receptor complex with doxepin
    • Shimamura T, Shiroishi M, Weyand S, et al. Structure of the human histamine H1 receptor complex with doxepin. Nature 2011 ; 475 : 65-70.
    • (2011) Nature , vol.475 , pp. 65-70
    • Shimamura, T.1    Shiroishi, M.2    Weyand, S.3
  • 8
    • 47949129742 scopus 로고    scopus 로고
    • Structure of a beta1-adrenergic g protein-coupled receptor
    • Warne T, Serrano-Vega MJ, Baker JG, et al. Structure of a beta1-adrenergic G protein-coupled receptor. Nature 2008 ; 454 : 486-91.
    • (2008) Nature , vol.454 , pp. 486-91
    • Warne, T.1    Serrano-Vega, M.J.2    Baker, J.G.3
  • 9
    • 78449305788 scopus 로고    scopus 로고
    • Structure of the human dopamine d3 receptor in complex with a d2/d3 selective antagonist
    • Chien EY, Liu W, Zhao Q, et al. Structure of the human dopamine D3 receptor in complex with a D2/D3 selective antagonist. Science 2010 ; 330 : 1091-5.
    • (2010) Science , vol.330 , pp. 1091-5
    • Chien, E.Y.1    Liu, W.2    Zhao, Q.3
  • 10
    • 85027927015 scopus 로고    scopus 로고
    • Structures of the cxcr4 chemokine gpcr with small-molecule and cyclic peptide antagonists
    • Wu B, Chien EY, Mol CD, et al. Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists. Science 2010 ; 330 : 1066-71.
    • (2010) Science , vol.330 , pp. 1066-71
    • Wu, B.1    Chien, E.Y.2    Mol, C.D.3
  • 11
    • 56749103466 scopus 로고    scopus 로고
    • The 2.6 angstrom crystal structure of a human a2a adenosine receptor bound to an antagonist
    • Jaakola VP, Griffith MT, Hanson MA, et al. The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist. Science 2008 ; 322 : 1211-7.
    • (2008) Science , vol.322 , pp. 1211-7
    • Jaakola, V.P.1    Griffith, M.T.2    Hanson, M.A.3
  • 14
    • 0035984890 scopus 로고    scopus 로고
    • Functional reconstitution of purified metabotropic glutamate receptor expressed in the fly eye
    • DOI 10.1093/embo-reports/kvf088
    • Eroglu C, Cronet P, Panneels V, et al. Functional reconstitution of purified metabotropic glutamate receptor expressed in the fly eye. EMBO Rep 2002 ; 3 : 491-6. (Pubitemid 34567439)
    • (2002) EMBO Reports , vol.3 , Issue.5 , pp. 491-496
    • Eroglu, C.1    Cronet, P.2    Panneels, V.3    Beaufils, P.4    Sinning, I.5
  • 15
    • 27644550921 scopus 로고    scopus 로고
    • Expression of functional G protein-coupled receptors in photoreceptors of transgenic Xenopus laevis
    • DOI 10.1021/bi051386z
    • Zhang L, Salom D, He J, et al. Expression of functional G protein-coupled receptors in photoreceptors of transgenic Xenopus laevis. Biochemistry 2005 ; 44 : 14509-18. (Pubitemid 41567459)
    • (2005) Biochemistry , vol.44 , Issue.44 , pp. 14509-14518
    • Zhang, L.1    Salom, D.2    He, J.3    Okun, A.4    Ballesteros, J.5    Palczewski, K.6    Li, N.7
  • 17
    • 77956188838 scopus 로고    scopus 로고
    • Modulation of g protein-coupled receptor sample quality by modified cell-free expression protocols: A case study of the human endothelin a receptor
    • Junge F, Luh LM, Proverbio D, et al. Modulation of G protein-coupled receptor sample quality by modified cell-free expression protocols: a case study of the human endothelin A receptor. J Struct Biol 2010 ; 172 : 94-106.
    • (2010) J Struct Biol , vol.172 , pp. 94-106
    • Junge, F.1    Luh, L.M.2    Proverbio, D.3
  • 18
    • 77950496251 scopus 로고    scopus 로고
    • Practical considerations of membrane protein instability during purification and crystallisation
    • Tate CG. Practical considerations of membrane protein instability during purification and crystallisation. Methods Mol Biol 2010 ; 601 : 187-203.
    • (2010) Methods Mol Biol , vol.601 , pp. 187-203
    • Tate, C.G.1
  • 19
    • 12244292640 scopus 로고    scopus 로고
    • 2a receptor functionally expressed in Escherichia coli
    • DOI 10.1046/j.0014-2956.2002.02618.x
    • Weiss HM, Grisshammer R. Purification and characterization of the human adenosine A(2a) receptor functionally expressed in Escherichia coli. Eur J Biochem 2002 ; 269 : 82-92. (Pubitemid 34107341)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.1 , pp. 82-92
    • Weiss, H.M.1    Grisshammer, R.2
  • 20
    • 71549138799 scopus 로고    scopus 로고
    • Purification of recombinant g protein-coupled receptors
    • Grisshammer R. Purification of recombinant G protein-coupled receptors. Methods Enzymol 2009 ; 463 : 631-45.
    • (2009) Methods Enzymol , vol.463 , pp. 631-45
    • Grisshammer, R.1
  • 21
    • 0038392702 scopus 로고    scopus 로고
    • 4 receptor BLT1 and the G-protein
    • DOI 10.1016/S0022-2836(03)00439-X
    • Banères JL, Parello J. Structure-based analysis of GPCR function: evidence for a novel pentameric assembly between the dimeric leukotriene B4 receptor BLT1 and the G protein. J Mol Biol 2003 ; 329 : 815-29. (Pubitemid 36629373)
    • (2003) Journal of Molecular Biology , vol.329 , Issue.4 , pp. 815-829
    • Baneres, J.-L.1    Parello, J.2
  • 22
    • 26444581283 scopus 로고    scopus 로고
    • Large-scale expression and purification of a G-protein-coupled receptor for structure determination - An overview
    • DOI 10.1007/s10969-005-1917-6
    • Grisshammer R, White JF, Trinh LB, Shiloach J. Large-scale expression and purification of a G protein-coupled receptor for structure determination: an overview. J Struct Funct Genomics 2005 ; 6 : 159-63. (Pubitemid 41428124)
    • (2005) Journal of Structural and Functional Genomics , vol.6 , Issue.2-3 , pp. 159-163
    • Grisshammer, R.1    White, J.F.2    Trinh, L.B.3    Shiloach, J.4
  • 24
    • 0023864252 scopus 로고
    • 2-adrenergic receptor in Chinese hamster fibroblasts (CHW): Functionality and regulation of the expressed receptors
    • Bouvier M, Hnatowich M, Collins S, et al. Expression of a human cDNA encoding the beta-2 adrenergic receptor in Chinese hamster fibroblasts (CHW): functionality and regulation of the expressed receptors. Mol Pharmacol 1988 ; 33 : 133-9. (Pubitemid 18068118)
    • (1988) Molecular Pharmacology , vol.33 , Issue.2 , pp. 133-139
    • Bouvier, M.1    Hnatowich, M.2    Collins, S.3    Kobilka, B.K.4    Deblasi, A.5    Lefkowitz, R.J.6    Caron, M.G.7
  • 25
    • 77958544093 scopus 로고    scopus 로고
    • Stability of the neurotensin receptor nts1 free in detergent solution and immobilized to affinity resin
    • White JF, Grisshammer R. Stability of the neurotensin receptor NTS1 free in detergent solution and immobilized to affinity resin. PLoS One 2010; 5 : 12579.
    • (2010) PLoS One , vol.5 , pp. 12579
    • White, J.F.1    Grisshammer, R.2
  • 26
    • 0027375525 scopus 로고
    • Characterization and purification of the solubilized pituitary adenylate-cyclase-activating polypeptide-1 receptor from porcine brain using a biotinylated ligand
    • DOI 10.1111/j.1432-1033.1993.tb18310.x
    • Schäfer H, Schmidt WE. Characterization and purification of the solubilized pituitary adenylatecyclase-activating polypeptide-1 receptor from porcine brain using a biotinylated ligand. Eur J Biochem 1993 ; 217 : 823-30. (Pubitemid 23326862)
    • (1993) European Journal of Biochemistry , vol.217 , Issue.3 , pp. 823-830
    • Schafer, H.1    Schmidt, W.E.2
  • 27
    • 0030467888 scopus 로고    scopus 로고
    • Expression of an olfactory receptor in Escherichia coli: Purification, reconstitution, and ligand binding
    • DOI 10.1021/bi9612069
    • Kiefer H, Krieger J, Olszewski JD, et al. Expression of an olfactory receptor in Escherichia coli: purification, reconstitution and ligand binding. Biochemistry 1996 ; 35 : 16077-84. (Pubitemid 27044069)
    • (1996) Biochemistry , vol.35 , Issue.50 , pp. 16077-16084
    • Kiefer, H.1    Krieger, J.2    Olszewski, J.D.3    Von Heijne, G.4    Prestwich, G.D.5    Breer, H.6
  • 28
    • 79959294939 scopus 로고    scopus 로고
    • New advances in production and functional folding of g protein-coupled receptors
    • Banères JL, Popot JL, Mouillac B. New advances in production and functional folding of G protein-coupled receptors. Trends Biotechnol 2011; 29 : 314-22.
    • (2011) Trends Biotechnol , vol.29 , pp. 314-322
    • Banères, J.L.1    Popot, J.L.2    Mouillac, B.3
  • 30
    • 79959564813 scopus 로고    scopus 로고
    • Agonist-bound adenosine a2a receptor structures reveal common features of gpcr activation
    • Lebon G, Warne T, Edwards PC, et al. Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation. Nature 2011 ; 474 : 521-5.
    • (2011) Nature , vol.474 , pp. 521-5
    • Lebon, G.1    Warne, T.2    Edwards, P.C.3
  • 31
    • 67349173167 scopus 로고    scopus 로고
    • Thermostabilization of the neurotensin receptor nts1
    • Shibata Y, White JF, Serrano-Vega MJ, et al. Thermostabilization of the neurotensin receptor NTS1. J Mol Biol 2009 ; 390 : 262-7.
    • (2009) J Mol Biol , vol.390 , pp. 262-7
    • Shibata, Y.1    White, J.F.2    Serrano-Vega, M.J.3
  • 32
    • 0037206131 scopus 로고    scopus 로고
    • Cholesterol as stabilizer of the oxytocin receptor
    • Gimpl G, Fahrenholz F. Cholesterol as stabilizer of the oxytocin receptor. Biochim Biophys Acta 2002 ; 1564 : 384-92.
    • (2002) Biochim Biophys Acta , vol.1564 , pp. 384-92
    • Gimpl, G.1    Fahrenholz, F.2
  • 33
    • 78649693871 scopus 로고    scopus 로고
    • Maltose-neopentyl glycol (mng) amphiphiles for solubilization, stabilization and crystallization of membrane proteins
    • Chae PS, Rasmussen SG, Rana RR, et al. Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins. Nat Methods 2010 ; 7 : 1003-8.
    • (2010) Nat Methods , vol.7 , pp. 1003-8
    • Chae, P.S.1    Rasmussen, S.G.2    Rana, R.R.3
  • 34
    • 80051658642 scopus 로고    scopus 로고
    • Crystal structure of the beta2 adrenergic receptor gs protein complex
    • Rasmussen SG, DeVree BT, Zou Y, et al. Crystal structure of the beta2 adrenergic receptor Gs protein complex. Nature 2011 ; 477 : 549-55.
    • (2011) Nature , vol.477 , pp. 549-55
    • Rasmussen, S.G.1    DeVree, B.T.2    Zou, Y.3
  • 35
    • 0032075801 scopus 로고    scopus 로고
    • Stabilization of integral membrane proteins in aqueous solution using fluorinated surfactants
    • DOI 10.1016/S0300-9084(00)80017-6
    • Chabaud, E, Barthélémy P, Mora N, et al. Stabilization of integral membrane proteins in aqueous solution using fluorinated surfactants. Biochimie 1998 ; 80 : 515-30. (Pubitemid 28425398)
    • (1998) Biochimie , vol.80 , Issue.5-6 , pp. 515-530
    • Chabaud, E.1    Barthelemy, P.2    Mora, N.3    Popot, J.L.4    Pucci, B.5
  • 36
    • 34247620784 scopus 로고    scopus 로고
    • New tensio-active molecules stabilize a human G protein-coupled receptor in solution
    • DOI 10.1016/j.febslet.2007.03.091, PII S0014579307003699
    • Damian M, Perino S, Polidori A, et al. New tensio-active molecules stabilize a human G protein-coupled receptor in solution. FEBS Lett 2007 ; 581 : 1944-50. (Pubitemid 46670118)
    • (2007) FEBS Letters , vol.581 , Issue.10 , pp. 1944-1950
    • Damian, M.1    Perino, S.2    Polidori, A.3    Martin, A.4    Serre, L.5    Pucci, B.6    Baneres, J.-L.7
  • 38
    • 77951903021 scopus 로고    scopus 로고
    • Membrane protein assembly into nanodiscs
    • Bayburt TH, Sligar SG. Membrane protein assembly into nanodiscs. FEBS Lett 2010 ; 584 : 1721-7.
    • (2010) FEBS Lett , vol.584 , pp. 1721-7
    • Bayburt, T.H.1    Sligar, S.G.2
  • 39
    • 34447509986 scopus 로고    scopus 로고
    • Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins
    • DOI 10.1074/jbc.M701433200
    • Bayburt TH, Leitz AJ, Xie G, et al. Transducin activation by nanoscale lipid bilayers containing one or two rhodopsins. J Biol Chem 2007; 282 : 14875-81. (Pubitemid 47093370)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.20 , pp. 14875-14881
    • Bayburt, T.H.1    Leitz, A.J.2    Xie, G.3    Oprian, D.D.4    Sligar, S.G.5
  • 41
    • 67650080503 scopus 로고    scopus 로고
    • Amphipol-assisted in vitro folding of g protein-coupled receptors
    • Dahmane T, Damian M, Mary S, et al. Amphipol-assisted in vitro folding of G protein-coupled receptors. Biochemistry 2009 ; 48 : 6516-21.
    • (2009) Biochemistry , vol.48 , pp. 6516-21
    • Dahmane, T.1    Damian, M.2    Mary, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.