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Volumn 56, Issue 6, 1999, Pages 1116-1126

Dopamine D4/D2 receptor selectivity is determined by a divergent aromatic microdomain contained within the second, third, and seventh membrane-spanning segments

Author keywords

[No Author keywords available]

Indexed keywords

DOPAMINE 2 RECEPTOR; DOPAMINE 4 RECEPTOR;

EID: 0032723795     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: 10.1124/mol.56.6.1116     Document Type: Article
Times cited : (95)

References (38)
  • 1
    • 0027987062 scopus 로고
    • Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the α subunit
    • Akabas MH, Kaufmann C, Archdeacon P and Karlin A (1984) Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the α subunit. Neuron 13:919-927.
    • (1984) Neuron , vol.13 , pp. 919-927
    • Akabas, M.H.1    Kaufmann, C.2    Archdeacon, P.3    Karlin, A.4
  • 2
    • 0026485739 scopus 로고
    • Acetylcholine receptor channel structure probed in cysteine-substitution mutante
    • Akabas MH, Stauffer DA, Xu M and Karlin A (1992) Acetylcholine receptor channel structure probed in cysteine-substitution mutante. Science (Wash DC) 258:307-310.
    • (1992) Science (Wash DC) , vol.258 , pp. 307-310
    • Akabas, M.H.1    Stauffer, D.A.2    Xu, M.3    Karlin, A.4
  • 3
    • 0029818551 scopus 로고    scopus 로고
    • Structural features and light-dependent changes in the cytoplasmic inter-helical E-F loop region of rhodopsin: A site-directed spin-labeling study
    • Altenbach C, Yang K, Farrens DL, Farahbakhsh ZT, Khorana HG and Hubbell WL (1996) Structural features and light-dependent changes in the cytoplasmic inter-helical E-F loop region of rhodopsin: A site-directed spin-labeling study. Biochemistry 35:12470-12478.
    • (1996) Biochemistry , vol.35 , pp. 12470-12478
    • Altenbach, C.1    Yang, K.2    Farrens, D.L.3    Farahbakhsh, Z.T.4    Khorana, H.G.5    Hubbell, W.L.6
  • 4
    • 0031565726 scopus 로고    scopus 로고
    • An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors
    • Baldwin JM, Schertler GF and Unger VM (1997) An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors. J Mol Biol 272:144-164.
    • (1997) J Mol Biol , vol.272 , pp. 144-164
    • Baldwin, J.M.1    Schertler, G.F.2    Unger, V.M.3
  • 6
    • 77957055780 scopus 로고
    • Integrated methods for modeling G-protein coupled receptors
    • Ballesteros JA and Weinstein H (1995) Integrated methods for modeling G-protein coupled receptors. Methods Neurosci 25:366-428.
    • (1995) Methods Neurosci , vol.25 , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 9
    • 0015861774 scopus 로고
    • Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (150) of an enzymatic reaction
    • Cheng Y and Prusoff WH (1973) Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (150) of an enzymatic reaction. Biochem Pharmacol 22:3099-3108.
    • (1973) Biochem Pharmacol , vol.22 , pp. 3099-3108
    • Cheng, Y.1    Prusoff, W.H.2
  • 10
    • 0028971630 scopus 로고
    • Hydrophobic residues of the D2 dopamine receptor are important for binding and signal transduction
    • Cho W, Taylor LP, Mansour A and Akil H (1995) Hydrophobic residues of the D2 dopamine receptor are important for binding and signal transduction. J Neurochem 65:2105-2115.
    • (1995) J Neurochem , vol.65 , pp. 2105-2115
    • Cho, W.1    Taylor, L.P.2    Mansour, A.3    Akil, H.4
  • 12
    • 0028906185 scopus 로고
    • Differential ergoline and ergopeptine binding to 5-hydroxytryptamine2A receptors: Ergolines require an aromatic residue at position 340 for high affinity binding
    • Choudhary MS, Sachs N, Uluer A, Glennon RA, Westkaemper RB and Roth BL (1995) Differential ergoline and ergopeptine binding to 5-hydroxytryptamine2A receptors: Ergolines require an aromatic residue at position 340 for high affinity binding. Mol Pharmacol 47:450-457.
    • (1995) Mol Pharmacol , vol.47 , pp. 450-457
    • Choudhary, M.S.1    Sachs, N.2    Uluer, A.3    Glennon, R.A.4    Westkaemper, R.B.5    Roth, B.L.6
  • 13
    • 0026729248 scopus 로고
    • Contributions of conserved serine residues to the interactions of ligands with dopamine D2 receptors
    • Cox BA, Henningsen RA, Spanoyannis A, Neve RL and Neve KA (1992) Contributions of conserved serine residues to the interactions of ligands with dopamine D2 receptors. J Neurochem 59:627-635.
    • (1992) J Neurochem , vol.59 , pp. 627-635
    • Cox, B.A.1    Henningsen, R.A.2    Spanoyannis, A.3    Neve, R.L.4    Neve, K.A.5
  • 14
    • 0029035661 scopus 로고
    • Mapping light-dependent structural changes in the cytoplasmic loop connecting helices C and D in rhodopsin: A site-directed spin labeling study
    • Farahbakhsh ZT, Ridge KD, Khorana HG and Hubbell WL (1995) Mapping light-dependent structural changes in the cytoplasmic loop connecting helices C and D in rhodopsin: A site-directed spin labeling study. Biochemistry 34:8812-8819.
    • (1995) Biochemistry , vol.34 , pp. 8812-8819
    • Farahbakhsh, Z.T.1    Ridge, K.D.2    Khorana, H.G.3    Hubbell, W.L.4
  • 15
    • 0029757635 scopus 로고    scopus 로고
    • Residues in the seventh membrane-spanning segment of the dopamine D2 receptor accessible in the binding-site crevice
    • Fu D, Ballesteros JA, Weinstein H, Chen J and Javitch JA (1996) Residues in the seventh membrane-spanning segment of the dopamine D2 receptor accessible in the binding-site crevice. Biochemistry 35:11278-11285.
    • (1996) Biochemistry , vol.35 , pp. 11278-11285
    • Fu, D.1    Ballesteros, J.A.2    Weinstein, H.3    Chen, J.4    Javitch, J.A.5
  • 17
    • 0033594927 scopus 로고    scopus 로고
    • Electrostatic and aromatic microdomains within the binding-site crevice of the D2 receptor: Contributions of the second membrane-spanning segment
    • Javitch JA, Ballesteros JA, Chen J, Chiappa V and Simpson MM (1999) Electrostatic and aromatic microdomains within the binding-site crevice of the D2 receptor: Contributions of the second membrane-spanning segment. Biochemistry 38:7961-7968.
    • (1999) Biochemistry , vol.38 , pp. 7961-7968
    • Javitch, J.A.1    Ballesteros, J.A.2    Chen, J.3    Chiappa, V.4    Simpson, M.M.5
  • 18
    • 0032570306 scopus 로고    scopus 로고
    • A cluster of aromatic residues in the sixth membrane-spanning segment of the dopamine D2 receptor is accessible in the binding-site crevice
    • Javitch JA, Ballesteros JA, Weinstein H and Chen J (1998) A cluster of aromatic residues in the sixth membrane-spanning segment of the dopamine D2 receptor is accessible in the binding-site crevice. Biochemistry 37:998-1006.
    • (1998) Biochemistry , vol.37 , pp. 998-1006
    • Javitch, J.A.1    Ballesteros, J.A.2    Weinstein, H.3    Chen, J.4
  • 19
    • 0029617613 scopus 로고
    • Residues in the fifth membrane-spanning segment of the dopamine D2 receptor exposed in the binding-site crevice
    • Javitch JA, Fu D and Chen J (1995a) Residues in the fifth membrane-spanning segment of the dopamine D2 receptor exposed in the binding-site crevice. Biochemistry 34:16433-16439.
    • (1995) Biochemistry , vol.34 , pp. 16433-16439
    • Javitch, J.A.1    Fu, D.2    Chen, J.3
  • 20
    • 0028920298 scopus 로고
    • Mapping the binding-site crevice of the dopamine D2 receptor by the substituted-cysteine accessibility method
    • Javitch JA, Fu D, Chen J and Karlin A (1995b) Mapping the binding-site crevice of the dopamine D2 receptor by the substituted-cysteine accessibility method. Neuron 14:825-831.
    • (1995) Neuron , vol.14 , pp. 825-831
    • Javitch, J.A.1    Fu, D.2    Chen, J.3    Karlin, A.4
  • 21
    • 0029021945 scopus 로고
    • Genetic transfer of a nonpeptide antagonist binding site to a previously unresponsive angiotensin receptor
    • Ji H, Zheng W, Zhang Y, Catt KJ and Sandberg K (1995) Genetic transfer of a nonpeptide antagonist binding site to a previously unresponsive angiotensin receptor. Proc Natl Acad Sci USA 92:9240-9244.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9240-9244
    • Ji, H.1    Zheng, W.2    Zhang, Y.3    Catt, K.J.4    Sandberg, K.5
  • 22
    • 0023889603 scopus 로고
    • Chimeric alpha 2-, beta 2-adrenergic receptors: Delineation of domains involved in effector coupling and ligand binding specificity
    • Kobilka BK, Kobilka TS, Daniel K, Regan JW, Caron MG and Lefkowitz RJ (1988) Chimeric alpha 2-, beta 2-adrenergic receptors: Delineation of domains involved in effector coupling and ligand binding specificity. Science (Wash DC) 240:1310-1316.
    • (1988) Science (Wash DC) , vol.240 , pp. 1310-1316
    • Kobilka, B.K.1    Kobilka, T.S.2    Daniel, K.3    Regan, J.W.4    Caron, M.G.5    Lefkowitz, R.J.6
  • 23
    • 0031439585 scopus 로고    scopus 로고
    • Constitutive activity of a chimeric D2/D1 dopamine receptor
    • Kozell LB and Neve KA (1997) Constitutive activity of a chimeric D2/D1 dopamine receptor. Mol Pharmacol 52:1137-1149.
    • (1997) Mol Pharmacol , vol.52 , pp. 1137-1149
    • Kozell, L.B.1    Neve, K.A.2
  • 24
    • 0029845242 scopus 로고    scopus 로고
    • A database of mutants and effects of site-directed mutagenesis experiments on G protein-coupled receptors
    • Kristiansen K, Dahl SG and Edvardsen O (1996) A database of mutants and effects of site-directed mutagenesis experiments on G protein-coupled receptors. Proteins 26:81-94.
    • (1996) Proteins , vol.26 , pp. 81-94
    • Kristiansen, K.1    Dahl, S.G.2    Edvardsen, O.3
  • 27
    • 0026772266 scopus 로고
    • The ligand-binding domain of rhodopsin and other G protein-linked receptors
    • Oprian DD (1992) The ligand-binding domain of rhodopsin and other G protein-linked receptors. J Bioenerget Biomemb 24:211-217.
    • (1992) J Bioenerget Biomemb , vol.24 , pp. 211-217
    • Oprian, D.D.1
  • 28
    • 0030027934 scopus 로고    scopus 로고
    • Bicistronic vector for the creation of stable mammalian cell lines that predisposes all antibiotic-resistant cells to express recombinant protein
    • Rees S, Coote J, Stables J, Goodson S, Harris S and Lee MG (1996) Bicistronic vector for the creation of stable mammalian cell lines that predisposes all antibiotic-resistant cells to express recombinant protein. BioTechniques 20:102-110.
    • (1996) BioTechniques , vol.20 , pp. 102-110
    • Rees, S.1    Coote, J.2    Stables, J.3    Goodson, S.4    Harris, S.5    Lee, M.G.6
  • 30
    • 0025179967 scopus 로고
    • Molecular cloning and characterization of a novel dopamine receptor (D3) as a target for neuroleptics
    • Sokoloff P, Giros B, Martres MP, Bouthenet ML and Schwartz JC (1990) Molecular cloning and characterization of a novel dopamine receptor (D3) as a target for neuroleptics. Nature (Lond) 347:146-151.
    • (1990) Nature (Lond) , vol.347 , pp. 146-151
    • Sokoloff, P.1    Giros, B.2    Martres, M.P.3    Bouthenet, M.L.4    Schwartz, J.C.5
  • 31
    • 0024344941 scopus 로고
    • Identification of two serine residues involved in agonist activation of the beta-adrenergic receptor
    • Strader CD, Candelore MR, Hill WS, Sigal IS and Dixon RA (1989) Identification of two serine residues involved in agonist activation of the beta-adrenergic receptor. J Biol Chem 264:13572-13578.
    • (1989) J Biol Chem , vol.264 , pp. 13572-13578
    • Strader, C.D.1    Candelore, M.R.2    Hill, W.S.3    Sigal, I.S.4    Dixon, R.A.5
  • 33
    • 0023740863 scopus 로고
    • Conserved aspartic acid residues 79 and 113 of the beta-adrenergic receptor have different roles in receptor function
    • Strader CD, Sigal IS, Candelore MR, Rands E, Hill WS and Dixon RA (1988) Conserved aspartic acid residues 79 and 113 of the beta-adrenergic receptor have different roles in receptor function. J Biol Chem 263:10367-10271.
    • (1988) J Biol Chem , vol.263 , pp. 10367-110271
    • Strader, C.D.1    Sigal, I.S.2    Candelore, M.R.3    Rands, E.4    Hill, W.S.5    Dixon, R.A.6
  • 34
    • 0029012098 scopus 로고
    • Interpretation of binding curves obtained with high receptor concentrations: Practical aid for computer analysis
    • Swillens S (1995) Interpretation of binding curves obtained with high receptor concentrations: Practical aid for computer analysis. Mol Pharmacol 47:1197-1203.
    • (1995) Mol Pharmacol , vol.47 , pp. 1197-1203
    • Swillens, S.1
  • 36
    • 0029919840 scopus 로고    scopus 로고
    • Molecular architecture of G protein-coupled receptors
    • Van Rhee AM and Jacobson KA (1996) Molecular architecture of G protein-coupled receptors. Drug Dev Res 37:1-38.
    • (1996) Drug Dev Res , vol.37 , pp. 1-38
    • Van Rhee, A.M.1    Jacobson, K.A.2
  • 38
    • 0028356148 scopus 로고
    • Identification of methionine134 and alaninel46 in the second transmembrane segment of the human tachykinin NK3 receptor as reduces involved in species-selective binding to SR 48968
    • Wu LH, Vartanian MA, Oxender DL and Chung FZ (1994) Identification of methionine134 and alaninel46 in the second transmembrane segment of the human tachykinin NK3 receptor as reduces involved in species-selective binding to SR 48968. Biochem Biophys Res Commun 198:961-966.
    • (1994) Biochem Biophys Res Commun , vol.198 , pp. 961-966
    • Wu, L.H.1    Vartanian, M.A.2    Oxender, D.L.3    Chung, F.Z.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.