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Volumn 105, Issue 3, 2008, Pages 877-882

Conformational thermostabilization of the β1-adrenergic receptor in a detergent-resistant form

Author keywords

G protein coupled receptor; Membrane protein; Stabilization

Indexed keywords

BETA 1 ADRENERGIC RECEPTOR; BETA ADRENERGIC RECEPTOR BLOCKING AGENT; DETERGENT; G PROTEIN COUPLED RECEPTOR; RHODOPSIN;

EID: 38949158505     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0711253105     Document Type: Article
Times cited : (380)

References (25)
  • 1
    • 3042621274 scopus 로고    scopus 로고
    • The progress of membrane protein structure determination
    • White SH (2004) The progress of membrane protein structure determination. Protein Sci 13:1948-1949.
    • (2004) Protein Sci , vol.13 , pp. 1948-1949
    • White, S.H.1
  • 2
    • 0035979797 scopus 로고    scopus 로고
    • Overexpression of mammalian integral membrane proteins for structural studies
    • Tate CG (2001) Overexpression of mammalian integral membrane proteins for structural studies. FEBS Lett 504:94-98.
    • (2001) FEBS Lett , vol.504 , pp. 94-98
    • Tate, C.G.1
  • 3
    • 0029142564 scopus 로고
    • Overexpression of integral membrane proteins for structural studies
    • Grisshammer R, Tate CG (1995) Overexpression of integral membrane proteins for structural studies. Q Rev Biophys 28:315-422.
    • (1995) Q Rev Biophys , vol.28 , pp. 315-422
    • Grisshammer, R.1    Tate, C.G.2
  • 4
    • 0035423934 scopus 로고    scopus 로고
    • Stabilizing membrane proteins
    • Bowie JU (2001) Stabilizing membrane proteins. Curr Opin Struct Biol 11:397-402.
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 397-402
    • Bowie, J.U.1
  • 5
    • 0033538418 scopus 로고    scopus 로고
    • Changing single side-chains can greatly enhance the resistance of a membrane protein to irreversible inactivation
    • Lau FW, Nauli S, Zhou Y, Bowie JU (1999) Changing single side-chains can greatly enhance the resistance of a membrane protein to irreversible inactivation. J Mol Biol 290:559-564.
    • (1999) J Mol Biol , vol.290 , pp. 559-564
    • Lau, F.W.1    Nauli, S.2    Zhou, Y.3    Bowie, J.U.4
  • 6
    • 0034629489 scopus 로고    scopus 로고
    • Building a thermostable membrane protein
    • Zhou Y, Bowie JU (2000) Building a thermostable membrane protein. J Biol Chem 275:6975-6979.
    • (2000) J Biol Chem , vol.275 , pp. 6975-6979
    • Zhou, Y.1    Bowie, J.U.2
  • 7
    • 0344687314 scopus 로고    scopus 로고
    • Side-chain contributions to membrane protein structure and stability
    • Faham S, et al. (2004) Side-chain contributions to membrane protein structure and stability. J Mol Biol 335:297-305.
    • (2004) J Mol Biol , vol.335 , pp. 297-305
    • Faham, S.1
  • 9
    • 0024999554 scopus 로고
    • A truncation mutation in the avian beta-adrenergic receptor causes agonist-induced internalization and GTP-sensitive agonist binding characteristic of mammalian receptors
    • Hertel C, et al. (1990) A truncation mutation in the avian beta-adrenergic receptor causes agonist-induced internalization and GTP-sensitive agonist binding characteristic of mammalian receptors. J Biol Chem 265:17988-17994.
    • (1990) J Biol Chem , vol.265 , pp. 17988-17994
    • Hertel, C.1
  • 10
    • 0037450576 scopus 로고    scopus 로고
    • Expression and purification of truncated, non-glycosylated turkey beta-adrenergic receptors for crystallization
    • Warne T, Chirnside J, Schertler GF (2003) Expression and purification of truncated, non-glycosylated turkey beta-adrenergic receptors for crystallization. Biochim Biophys Acta 1610:133-140.
    • (2003) Biochim Biophys Acta , vol.1610 , pp. 133-140
    • Warne, T.1    Chirnside, J.2    Schertler, G.F.3
  • 11
    • 0025836218 scopus 로고
    • Truncation of the extended carboxyl-terminal domain increases the expression and regulatory activity of the avian beta-adrenergic receptor
    • Parker EM, Ross EM (1991) Truncation of the extended carboxyl-terminal domain increases the expression and regulatory activity of the avian beta-adrenergic receptor. J Biol Chem 266:9987-9996.
    • (1991) J Biol Chem , vol.266 , pp. 9987-9996
    • Parker, E.M.1    Ross, E.M.2
  • 12
    • 0026086012 scopus 로고
    • Reconstitutively active G protein-coupled receptors purified from baculovirus-infected insect cells
    • Parker EM, Kameyama K, Higashijima T, Ross EM (1991) Reconstitutively active G protein-coupled receptors purified from baculovirus-infected insect cells. J Biol Chem 266:519-527.
    • (1991) J Biol Chem , vol.266 , pp. 519-527
    • Parker, E.M.1    Kameyama, K.2    Higashijima, T.3    Ross, E.M.4
  • 13
    • 0020017112 scopus 로고
    • Thermal stability of rhodopsin and opsin in some novel detergents
    • Degrip WJ (1982) Thermal stability of rhodopsin and opsin in some novel detergents. Methods Enzymol 81:256-265.
    • (1982) Methods Enzymol , vol.81 , pp. 256-265
    • Degrip, W.J.1
  • 14
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G protein-coupled receptor
    • Palczewski K, et al. (2000) Crystal structure of rhodopsin: A G protein-coupled receptor. Science 289:739-745.
    • (2000) Science , vol.289 , pp. 739-745
    • Palczewski, K.1
  • 16
    • 33745172476 scopus 로고    scopus 로고
    • Rezmann-Vitti LA, et al. (2006) Role of Tyr(356(7.43)) and Ser(190(4.57)) in antagonist binding in the rat beta1-adrenergic receptor. J Med Chem 49:3467-3477.
    • Rezmann-Vitti LA, et al. (2006) Role of Tyr(356(7.43)) and Ser(190(4.57)) in antagonist binding in the rat beta1-adrenergic receptor. J Med Chem 49:3467-3477.
  • 17
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • Abramson J, et al. (2003) Structure and mechanism of the lactose permease of Escherichia coli. Science 301:610-615.
    • (2003) Science , vol.301 , pp. 610-615
    • Abramson, J.1
  • 18
    • 36248970132 scopus 로고    scopus 로고
    • Crystal structure of the human beta(2) adrenergic G-protein-coupled receptor
    • Rasmussen SG, et al. (2007) Crystal structure of the human beta(2) adrenergic G-protein-coupled receptor. Nature 15:383-387.
    • (2007) Nature , vol.15 , pp. 383-387
    • Rasmussen, S.G.1
  • 19
    • 36448995359 scopus 로고    scopus 로고
    • High-resolution crystal structure of an engineered human β2-adrenergic G protein coupled receptor
    • Cherezov V, et al. (2007) High-resolution crystal structure of an engineered human β2-adrenergic G protein coupled receptor. Science 318:1258-1265.
    • (2007) Science , vol.318 , pp. 1258-1265
    • Cherezov, V.1
  • 20
    • 0018874760 scopus 로고
    • A comparison of the beta-adrenergic receptor of the turkey erythrocyte with mammalian beta1 and beta2 receptors
    • Minneman KP, Weiland GA, Molinoff PB (1980) A comparison of the beta-adrenergic receptor of the turkey erythrocyte with mammalian beta1 and beta2 receptors. Mol Pharmacol 17:1-7.
    • (1980) Mol Pharmacol , vol.17 , pp. 1-7
    • Minneman, K.P.1    Weiland, G.A.2    Molinoff, P.B.3
  • 21
    • 0028948741 scopus 로고
    • Carboxyl-terminal domains in the avian beta 1-adrenergic receptor that regulate agonist-promoted endocytosis
    • Parker EM, Swigart P, Nunnally MH, Perkins JP, Ross EM (1995) Carboxyl-terminal domains in the avian beta 1-adrenergic receptor that regulate agonist-promoted endocytosis. J Biol Chem 270:6482-6487.
    • (1995) J Biol Chem , vol.270 , pp. 6482-6487
    • Parker, E.M.1    Swigart, P.2    Nunnally, M.H.3    Perkins, J.P.4    Ross, E.M.5
  • 22
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • Jaenicke R, Bohm G (1998) The stability of proteins in extreme environments. Curr Opin Struct Biol 8:738-748.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 738-748
    • Jaenicke, R.1    Bohm, G.2
  • 23
    • 0029838532 scopus 로고    scopus 로고
    • Purification of a rat neurotensin receptor expressed in Escherichia coli
    • Tucker J, Grisshammer R (1996) Purification of a rat neurotensin receptor expressed in Escherichia coli. Biochem J 317:891-899.
    • (1996) Biochem J , vol.317 , pp. 891-899
    • Tucker, J.1    Grisshammer, R.2
  • 25
    • 12244292640 scopus 로고    scopus 로고
    • Purification and characterization of the human adenosine A (2a) receptor functionally expressed in Escherichia coli
    • Weiss HM, Grisshammer R (2002) Purification and characterization of the human adenosine A (2a) receptor functionally expressed in Escherichia coli. Eur J Biochem 269:82-92.
    • (2002) Eur J Biochem , vol.269 , pp. 82-92
    • Weiss, H.M.1    Grisshammer, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.