메뉴 건너뛰기




Volumn 50, Issue 5, 1996, Pages 1338-1345

Mutagenesis of residues adjacent to transmembrane prolines alters D1 dopamine receptor binding and signal transduction

Author keywords

[No Author keywords available]

Indexed keywords

DOPAMINE 1 RECEPTOR; PROLINE;

EID: 0029829503     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (26)

References (40)
  • 3
    • 0023740863 scopus 로고
    • Conserved aspartate residues 79 and 113 of the β-adrenergic receptor have different roles in receptor function
    • Strader, C. D., I. S. Sigal, M. R. Candelore, E. Rands, W. S. Hill, and R. A. F. Dixon. Conserved aspartate residues 79 and 113 of the β-adrenergic receptor have different roles in receptor function. J. Biol. Chem. 263: 10267-10271 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 10267-10271
    • Strader, C.D.1    Sigal, I.S.2    Candelore, M.R.3    Rands, E.4    Hill, W.S.5    Dixon, R.A.F.6
  • 6
    • 0024344941 scopus 로고
    • Identification of two serine residues involved in agonist activation of the β-adrenergic receptor
    • Strader, C. D., M. R. Candelore, W. S. Hill, I. S. Sigal, and R. A. F. Dixon. Identification of two serine residues involved in agonist activation of the β-adrenergic receptor. J. Biol. Chem. 264:13572-13578 (1989).
    • (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.F.5
  • 12
    • 0025817671 scopus 로고
    • 2A-adrenergic receptor alter receptor-G protein coupling by distinct mechanisms
    • 2A-adrenergic receptor alter receptor-G protein coupling by distinct mechanisms. J. Biol. Chem. 266:11025-11029 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 11025-11029
    • Dalman, H.M.1    Neubig, R.R.2
  • 13
    • 0026660322 scopus 로고
    • Modeling of G-protein-coupled receptors: Applications to dopamine, adrenaline, serotonin, acetylcholine, and mammalian opsin receptors
    • Trumpp-Kallmeyer, S., J. Hoflack, A. Bruinvels, and M. Hibert. Modeling of G-protein-coupled receptors: applications to dopamine, adrenaline, serotonin, acetylcholine, and mammalian opsin receptors. J. Med. Chem. 35:3448-3462 (1992).
    • (1992) J. Med. Chem. , vol.35 , pp. 3448-3462
    • Trumpp-Kallmeyer, S.1    Hoflack, J.2    Bruinvels, A.3    Hibert, M.4
  • 14
    • 0025292355 scopus 로고
    • Model of the structure of bacteriorhodopsin based on high resolution electron cryomicroscopy
    • Henderson, R., J. Baldwin, T. H. Ceska, F. Zemlin, E. Beckmann, and K. Downing. Model of the structure of bacteriorhodopsin based on high resolution electron cryomicroscopy. J. Mol. Biol. 213:899-929 (1990).
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.2    Ceska, T.H.3    Zemlin, F.4    Beckmann, E.5    Downing, K.6
  • 15
    • 0014432828 scopus 로고
    • Conformational energies and configurational statistics of copolypeptides containing L-proline
    • Schimmel, P. R., and P. J. Flory. Conformational energies and configurational statistics of copolypeptides containing L-proline. J. Mol. Biol. 34: 105-120 (1968).
    • (1968) J. Mol. Biol. , vol.34 , pp. 105-120
    • Schimmel, P.R.1    Flory, P.J.2
  • 16
    • 0025890946 scopus 로고
    • Influence of proline residues on protein conformation
    • MacArthur, M. W., and J. M. Thornton. Influence of proline residues on protein conformation. J. Mol. Biol. 218:397-412 (1991).
    • (1991) J. Mol. Biol. , vol.218 , pp. 397-412
    • MacArthur, M.W.1    Thornton, J.M.2
  • 17
    • 0025945775 scopus 로고
    • Proline residues in transmembrane helices: Structural or dynamic role?
    • Williams, K. A., and C. M. Deber. Proline residues in transmembrane helices: structural or dynamic role? Biochemistry 30:8919-8923 (1991).
    • (1991) Biochemistry , vol.30 , pp. 8919-8923
    • Williams, K.A.1    Deber, C.M.2
  • 18
    • 10544251337 scopus 로고
    • Conformational energy of proline-containing peptides in a non-polar environment
    • (E. Giralt and D. Andreu, eds.). ESCOM Science Publishers, Leiden
    • Deber, C. M., A. Polinsky, and M. Goodman. Conformational energy of proline-containing peptides in a non-polar environment, in Peptides 1990 (E. Giralt and D. Andreu, eds.). Vol. 10. ESCOM Science Publishers, Leiden, 485-487 (1991).
    • (1991) Peptides 1990 , vol.10 , pp. 485-487
    • Deber, C.M.1    Polinsky, A.2    Goodman, M.3
  • 19
    • 0000882208 scopus 로고
    • Hypothesis about the function of membrane-buried proline residues in transport proteins
    • Brandi, C. J., and C. M. Deber. Hypothesis about the function of membrane-buried proline residues in transport proteins. Proc. Natl. Acad. Sci. USA 83:917-921 (1986).
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 917-921
    • Brandi, C.J.1    Deber, C.M.2
  • 21
    • 0016711868 scopus 로고
    • Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues
    • Brandts, J. F., H. R. Halvorson, and M. Brennan. Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. Biochemistry 14:4953-4963 (1975).
    • (1975) Biochemistry , vol.14 , pp. 4953-4963
    • Brandts, J.F.1    Halvorson, H.R.2    Brennan, M.3
  • 22
    • 84985715908 scopus 로고
    • Isomerization in oligopeptides
    • Grathwohl. C., and K. Würtrich. Isomerization in oligopeptides. Biopolymers 20:2623-2633 (1981).
    • (1981) Biopolymers , vol.20 , pp. 2623-2633
    • Grathwohl, C.1    Würtrich, K.2
  • 23
    • 0023392945 scopus 로고
    • High-efficiency transformation of mammalian cells by plasmid DNA
    • Chen, C., and H. Okayama. High-efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell. Biol. 7:2745-2752 (1987).
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 24
    • 0019061918 scopus 로고
    • LIGAND: A versatile computerized approach for characterization of ligand-binding systems
    • Munson, P. J., and D. Rodbard. LIGAND: a versatile computerized approach for characterization of ligand-binding systems. Anal. Biochem. 107:220-239 (1980).
    • (1980) Anal. Biochem. , vol.107 , pp. 220-239
    • Munson, P.J.1    Rodbard, D.2
  • 28
    • 0028971630 scopus 로고
    • 2 dopamine receptor are important for binding and signal transduction
    • 2 dopamine receptor are important for binding and signal transduction. J. Neurochem. 66:2105-2115 (1995).
    • (1995) J. Neurochem. , vol.66 , pp. 2105-2115
    • Cho, W.1    Taylor, L.P.2    Mansour, A.3    Akil, H.4
  • 29
    • 0027297275 scopus 로고
    • Constitutive activity of receptors coupled to guanine nucleotide regulatory proteins
    • Lefkowitz, R. J., S. Cotecchia, P. Samana, and T. Costa. Constitutive activity of receptors coupled to guanine nucleotide regulatory proteins. Trends Pharmacol. Sci. 14:303-307 (1993).
    • (1993) Trends Pharmacol. Sci. , vol.14 , pp. 303-307
    • Lefkowitz, R.J.1    Cotecchia, S.2    Samana, P.3    Costa, T.4
  • 30
    • 0025212680 scopus 로고
    • 1-adrenergic receptor involved in coupling to phosphatidylinositol hydrolysis and enhanced sensitivity of biological function
    • 1-adrenergic receptor involved in coupling to phosphatidylinositol hydrolysis and enhanced sensitivity of biological function. Proc. Natl. Acad. Sci. USA 87:2896-2990 (1990).
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2896-2990
    • Cotecchia, S.1    Exum, S.2    Caron, M.3    Lefkowitz, R.4
  • 34
    • 0027372340 scopus 로고
    • A constitutively activating mutation of the luteinizing hormone receptor in familial male precocious puberty
    • Shenker, A., L. Laue, S. Kosugi, J. J. Merndino, Jr., T. Minegishi, and G. B. Cutler, Jr. A constitutively activating mutation of the luteinizing hormone receptor in familial male precocious puberty. Nature (Lond.) 365: 652-654 (1993).
    • (1993) Nature (Lond.) , vol.365 , pp. 652-654
    • Shenker, A.1    Laue, L.2    Kosugi, S.3    Merndino Jr., J.J.4    Minegishi, T.5    Cutler Jr., G.B.6
  • 36
    • 0027413475 scopus 로고
    • Pigmentation phenotypes of variant extension locus alleles result from point mutations that alter MSH receptor function
    • Robbins, L. S., J. H. Nadeau, K. R. Johnson, M. A. Kelly, L. Roselli-Rehfuss, E. Baack, K. G. Mountjoy, and R. D. Cone. Pigmentation phenotypes of variant extension locus alleles result from point mutations that alter MSH receptor function. Cell 72:827-834 (1993).
    • (1993) Cell , vol.72 , pp. 827-834
    • Robbins, L.S.1    Nadeau, J.H.2    Johnson, K.R.3    Kelly, M.A.4    Roselli-Rehfuss, L.5    Baack, E.6    Mountjoy, K.G.7    Cone, R.D.8
  • 38
    • 0025157643 scopus 로고
    • Proline residues undergo structural changes during proton pumping in bacteriorhodopsin
    • Gerwert, K, B. Hess, and M. Engelhard. Proline residues undergo structural changes during proton pumping in bacteriorhodopsin. FEBS Lett. 261:449-454 (1990).
    • (1990) FEBS Lett. , vol.261 , pp. 449-454
    • Gerwert, K.1    Hess, B.2    Engelhard, M.3
  • 39
    • 0024978498 scopus 로고
    • Structure-function studies on bacteriorhodopsin. VIII. Substitutions of the membrane-embedded pralines 50, 91, and 186: The effects are determined by the substituting amino acids
    • Mogi, T., L. J. Stern, B. H. Chao, and H. G. Khorana. Structure-function studies on bacteriorhodopsin. VIII. Substitutions of the membrane-embedded pralines 50, 91, and 186: the effects are determined by the substituting amino acids. J. Biol. Chem. 264:14192-14196 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 14192-14196
    • Mogi, T.1    Stern, L.J.2    Chao, B.H.3    Khorana, H.G.4
  • 40
    • 0027533339 scopus 로고
    • Functional role of proline and tryptophan residues highly conserved among G protein-coupled receptors studied by mutational analysis of the m3 muscarinic receptor
    • Wess, J., S. Nanavati, Z. Vogel, and R. Maggio. Functional role of proline and tryptophan residues highly conserved among G protein-coupled receptors studied by mutational analysis of the m3 muscarinic receptor. EMBO J. 12:331-338 (1993).
    • (1993) EMBO J. , vol.12 , pp. 331-338
    • Wess, J.1    Nanavati, S.2    Vogel, Z.3    Maggio, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.