메뉴 건너뛰기




Volumn 45, Issue 4, 2008, Pages 361-372

The role of proline residues in the structure and function of human MT2 melatonin receptor

Author keywords

G protein coupled melatonin receptors; Molecular dynamics; MT2 melatonin receptor; Proline

Indexed keywords

ALANINE; GLYCINE; GUANOSINE 5' O (3 THIOTRIPHOSPHATE) S 35; IODOMELATONIN I 125; MELATONIN 2 RECEPTOR; PROLINE; RADIOISOTOPE; RHODOPSIN; UNCLASSIFIED DRUG;

EID: 53749093762     PISSN: 07423098     EISSN: 1600079X     Source Type: Journal    
DOI: 10.1111/j.1600-079X.2008.00598.x     Document Type: Article
Times cited : (22)

References (58)
  • 1
    • 0031821519 scopus 로고    scopus 로고
    • Cellular mechanisms of melatonin action
    • Vanecek J. Cellular mechanisms of melatonin action. Physiol Rev 1998 78 : 687 721.
    • (1998) Physiol Rev , vol.78 , pp. 687-721
    • Vanecek, J.1
  • 2
    • 0023698530 scopus 로고
    • Effects of the pineal hormone melatonin on the proliferation and morphological characteristics of human breast cancer cells (MCF-7) in culture
    • Hill SM, Blask DE. Effects of the pineal hormone melatonin on the proliferation and morphological characteristics of human breast cancer cells (MCF-7) in culture. Cancer Res 1988 48 : 6121 6126.
    • (1988) Cancer Res , vol.48 , pp. 6121-6126
    • Hill, S.M.1    Blask, D.E.2
  • 3
    • 33845536018 scopus 로고    scopus 로고
    • One molecule, many derivatives: A never-ending interaction of melatonin with reactive oxygen and nitrogen species?
    • Tan DX, Manchester LC, Terron MP et al. One molecule, many derivatives: a never-ending interaction of melatonin with reactive oxygen and nitrogen species? J Pineal Res 2007 42 : 28 42.
    • (2007) J Pineal Res , vol.42 , pp. 28-42
    • Tan, D.X.1    Manchester, L.C.2    Terron, M.P.3
  • 4
    • 0028018966 scopus 로고
    • Cloning and characterization of a mammalian melatonin receptor that mediates reproductive and circadian responses
    • Reppert SM, Weaver DR, Ebisawa T. Cloning and characterization of a mammalian melatonin receptor that mediates reproductive and circadian responses. Neuron 1994 13 : 1177 1185.
    • (1994) Neuron , vol.13 , pp. 1177-1185
    • Reppert, S.M.1    Weaver, D.R.2    Ebisawa, T.3
  • 5
    • 0029115639 scopus 로고
    • Molecular characterization of a second melatonin receptor expressed in human retina and brain: The Mel1b melatonin receptor
    • Reppert SM, Godson C, Mahle CD et al. Molecular characterization of a second melatonin receptor expressed in human retina and brain: the Mel1b melatonin receptor. Proc Natl Acad Sci U S A 1995 92 : 8734 8738.
    • (1995) Proc Natl Acad Sci U S a , vol.92 , pp. 8734-8738
    • Reppert, S.M.1    Godson, C.2    Mahle, C.D.3
  • 6
    • 0025994321 scopus 로고
    • Vasoactive intestinal peptide stimulates catecholamine biosynthesis in isolated adrenal chromaffin cells: Evidence for a cyclic AMP-dependent phosphorylation and activation of tyrosine hydroxylase
    • Waymire JC, Craviso GL, Lichteig K et al. Vasoactive intestinal peptide stimulates catecholamine biosynthesis in isolated adrenal chromaffin cells: evidence for a cyclic AMP-dependent phosphorylation and activation of tyrosine hydroxylase. J Neurochem 1991 57 : 1313 1324.
    • (1991) J Neurochem , vol.57 , pp. 1313-1324
    • Waymire, J.C.1    Craviso, G.L.2    Lichteig, K.3
  • 7
    • 0035499604 scopus 로고    scopus 로고
    • The hunchback and its neighbours: Proline as an environmental modulator
    • Reiersen H, Rees AR. The hunchback and its neighbours: proline as an environmental modulator. Trends Biochem Sci 2001 26 : 679 684.
    • (2001) Trends Biochem Sci , vol.26 , pp. 679-684
    • Reiersen, H.1    Rees, A.R.2
  • 8
    • 0028600609 scopus 로고
    • Ligand-induced domain motion in the activation mechanism of a G-protein-coupled receptor
    • Luo X, Zhang D, Weinstein H. Ligand-induced domain motion in the activation mechanism of a G-protein-coupled receptor. Protein Eng 1994 7 : 1441 1448.
    • (1994) Protein Eng , vol.7 , pp. 1441-1448
    • Luo, X.1    Zhang, D.2    Weinstein, H.3
  • 9
    • 0036240805 scopus 로고    scopus 로고
    • A protein sequence that can encode native structure by disfavoring alternate conformations
    • Wigley WC, Corboy MJ, Cutler TD et al. A protein sequence that can encode native structure by disfavoring alternate conformations. Nat Struct Biol 2002 9 : 381 388.
    • (2002) Nat Struct Biol , vol.9 , pp. 381-388
    • Wigley, W.C.1    Corboy, M.J.2    Cutler, T.D.3
  • 10
    • 77957055780 scopus 로고
    • Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptors
    • Ballesteros JA, Weinstein H. Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptors. Methods Neurosci 1995 25 : 366 428.
    • (1995) Methods Neurosci , vol.25 , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 11
    • 0025761854 scopus 로고
    • Mapping of the amino acids in membrane-embedded helices that interact with the retinal chromophore in bovine rhodopsin
    • Nakayama TA, Khorana HG. Mapping of the amino acids in membrane-embedded helices that interact with the retinal chromophore in bovine rhodopsin. J Biol Chem 1991 266 : 4269 4275.
    • (1991) J Biol Chem , vol.266 , pp. 4269-4275
    • Nakayama, T.A.1    Khorana, H.G.2
  • 12
    • 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, Nanavati S, Vogel Z et al. 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 1993 12 : 331 338.
    • (1993) EMBO J , vol.12 , pp. 331-338
    • Wess, J.1    Nanavati, S.2    Vogel, Z.3
  • 13
    • 0029046606 scopus 로고
    • Probing the "message:address" sites for chemoattractant binding to the C5a receptor. Mutagenesis of hydrophilic and proline residues within the transmembrane segments
    • Kolakowski LF Jr., Lu B, Gerard C et al. Probing the "message: address" sites for chemoattractant binding to the C5a receptor. Mutagenesis of hydrophilic and proline residues within the transmembrane segments. J Biol Chem 1995 270 : 18077 18082.
    • (1995) J Biol Chem , vol.270 , pp. 18077-18082
    • Kolakowski Jr., L.F.1    Lu, B.2    Gerard, C.3
  • 14
    • 0036235905 scopus 로고    scopus 로고
    • The critical role of transmembrane prolines in human prostacyclin receptor activation
    • Stitham J, Martin KA, Hwa J. The critical role of transmembrane prolines in human prostacyclin receptor activation. Mol Pharmacol 2002 61 : 1202 1210.
    • (2002) Mol Pharmacol , vol.61 , pp. 1202-1210
    • Stitham, J.1    Martin, K.A.2    Hwa, J.3
  • 15
    • 0031047328 scopus 로고    scopus 로고
    • Roles of transmembrane prolines and proline-induced kinks of the lutropin/choriogonadotropin receptor
    • Hong S, Ryu KS, Oh MS et al. Roles of transmembrane prolines and proline-induced kinks of the lutropin/choriogonadotropin receptor. J Biol Chem 1997 272 : 4166 4171.
    • (1997) J Biol Chem , vol.272 , pp. 4166-4171
    • Hong, S.1    Ryu, K.S.2    Oh, M.S.3
  • 16
    • 0035851193 scopus 로고    scopus 로고
    • The role and predicted propensity of conserved proline residues in the 5-HT3 receptor
    • Deane CM, Lummis SC. The role and predicted propensity of conserved proline residues in the 5-HT3 receptor. J Biol Chem 2001 276 : 37962 37966.
    • (2001) J Biol Chem , vol.276 , pp. 37962-37966
    • Deane, C.M.1    Lummis, S.C.2
  • 17
    • 11244331476 scopus 로고    scopus 로고
    • A key role for transmembrane prolines in calcitonin receptor-like receptor agonist binding and signalling: Implications for family B G-protein-coupled receptors
    • Conner AC, Hay DL, Simms J et al. A key role for transmembrane prolines in calcitonin receptor-like receptor agonist binding and signalling: implications for family B G-protein-coupled receptors. Mol Pharmacol 2005 67 : 20 31.
    • (2005) Mol Pharmacol , vol.67 , pp. 20-31
    • Conner, A.C.1    Hay, D.L.2    Simms, J.3
  • 18
    • 0034787251 scopus 로고    scopus 로고
    • Three-dimensional representations of G protein-coupled receptor structures and mechanisms
    • Visiers I, Ballesteros JA, Weinstein H. Three-dimensional representations of G protein-coupled receptor structures and mechanisms. Methods Enzymol 2002 343 : 329 371.
    • (2002) Methods Enzymol , vol.343 , pp. 329-371
    • Visiers, I.1    Ballesteros, J.A.2    Weinstein, H.3
  • 19
    • 20844445439 scopus 로고    scopus 로고
    • Molecular modeling of human MT2 melatonin receptor: The role of Val204, Leu272 and Tyr298 in ligand binding
    • Mazna P, Obsilova V, Jelinkova I et al. Molecular modeling of human MT2 melatonin receptor: the role of Val204, Leu272 and Tyr298 in ligand binding. J Neurochem 2004 91 : 836 842.
    • (2004) J Neurochem , vol.91 , pp. 836-842
    • Mazna, P.1    Obsilova, V.2    Jelinkova, I.3
  • 20
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976 72 : 248 254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 21
    • 0028051828 scopus 로고
    • Derivation of rules for comparative protein modeling from a database of protein structure alignments
    • Sali A, Overington JP. Derivation of rules for comparative protein modeling from a database of protein structure alignments. Protein Sci 1994 3 : 1582 1596.
    • (1994) Protein Sci , vol.3 , pp. 1582-1596
    • Sali, A.1    Overington, J.P.2
  • 22
    • 4344581120 scopus 로고    scopus 로고
    • The retinal conformation and its environment in rhodopsin in light of a new 2.2 a crystal structure
    • Okada T, Sugihara M, Bondar et al. The retinal conformation and its environment in rhodopsin in light of a new 2.2 A crystal structure. J Mol Biol 2004 342 : 571 583.
    • (2004) J Mol Biol , vol.342 , pp. 571-583
    • Okada, T.1    Sugihara, M.2    Bondar3
  • 23
    • 0042121237 scopus 로고    scopus 로고
    • Multiple sequence alignment with the Clustal series of programs
    • Chenna R, Sugawara H, Koike T et al. Multiple sequence alignment with the Clustal series of programs. Nucleic Acids Res 2003 31 : 3497 3500.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3497-3500
    • Chenna, R.1    Sugawara, H.2    Koike, T.3
  • 24
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G protein-coupled receptor
    • Palczewski K, Kumasaka T, Hori T et al. Crystal structure of rhodopsin: a G protein-coupled receptor. Science 2000 289 : 739 745.
    • (2000) Science , vol.289 , pp. 739-745
    • Palczewski, K.1    Kumasaka, T.2    Hori, T.3
  • 25
    • 20444363062 scopus 로고    scopus 로고
    • Analysis of structure-activity relationships for MT2 selective antagonists by melatonin MT1 and MT2 receptor models
    • Rivara S, Lorenzi S, Mor M et al. Analysis of structure-activity relationships for MT2 selective antagonists by melatonin MT1 and MT2 receptor models. J Med Chem 2005 48 : 4049 4060.
    • (2005) J Med Chem , vol.48 , pp. 4049-4060
    • Rivara, S.1    Lorenzi, S.2    Mor, M.3
  • 26
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N, Peitsch MC. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 1997 18 : 2714 2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 27
    • 0030158429 scopus 로고    scopus 로고
    • PRODRG, a program for generating molecular topologies and unique molecular descriptors from coordinates of small molecules
    • Van Aalten DM, Bywater R, Findlay JB et al. PRODRG, a program for generating molecular topologies and unique molecular descriptors from coordinates of small molecules. J Comput Aided Mol Des 1996 10 : 255 262.
    • (1996) J Comput Aided Mol des , vol.10 , pp. 255-262
    • Van Aalten, D.M.1    Bywater, R.2    Findlay, J.B.3
  • 28
    • 0030203710 scopus 로고    scopus 로고
    • Distributed automated docking of flexible ligands to proteins: Parallel applications of AutoDock 2.4
    • Morris GM, Goodsell DS, Huey R et al. Distributed automated docking of flexible ligands to proteins: parallel applications of AutoDock 2.4. J Comput Aided Mol Des 1996 10 : 293 304.
    • (1996) J Comput Aided Mol des , vol.10 , pp. 293-304
    • Morris, G.M.1    Goodsell, D.S.2    Huey, R.3
  • 29
    • 0029633168 scopus 로고
    • GROMACS: A message-passing parallel molecular dynamics implementation
    • Berendsen HJC, Van Der Spoel D, Van Drunen R. GROMACS: A message-passing parallel molecular dynamics implementation. Comp Phys Comm 1995 91 : 43 56.
    • (1995) Comp Phys Comm , vol.91 , pp. 43-56
    • Berendsen, H.J.C.1    Van Der Spoel, D.2    Van Drunen, R.3
  • 30
    • 0026655361 scopus 로고
    • Stereochemical quality of protein structure coordinates
    • Morris AL, Macarthur MW, Hutchinson EG et al. Stereochemical quality of protein structure coordinates. Proteins 1992 12 : 345 364.
    • (1992) Proteins , vol.12 , pp. 345-364
    • Morris, A.L.1    MacArthur, M.W.2    Hutchinson, E.G.3
  • 31
    • 0031860932 scopus 로고    scopus 로고
    • A molecular dynamics study of the pores formed by Escherichia coli OmpF porin in a fully hydrated palmitoyloleoylphosphatidylcholine bilayer
    • Tieleman DP, Berendsen HJ. A molecular dynamics study of the pores formed by Escherichia coli OmpF porin in a fully hydrated palmitoyloleoylphosphatidylcholine bilayer. Biophys J 1998 74 : 2786 2801.
    • (1998) Biophys J , vol.74 , pp. 2786-2801
    • Tieleman, D.P.1    Berendsen, H.J.2
  • 32
    • 0002775934 scopus 로고
    • Interaction models for water in relation to protein hydration
    • In: Pullman, B. ed., Reidel, Dordrecht, pp.
    • Berendsen HJC, Postma JPM, Van Gunsteren WF et al. Interaction models for water in relation to protein hydration. In : Intermolecular Forces. Pullman B ed., Reidel, Dordrecht, 1981 pp. 331 342.
    • (1981) Intermolecular Forces. , pp. 331-342
    • Berendsen, H.J.C.1    Postma, J.P.M.2    Van Gunsteren, W.F.3
  • 33
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • Hess B, Bekker H, Berendsen HJC et al. LINCS: a linear constraint solver for molecular simulations. J Comput Chem 1997 18 : 1463 1472.
    • (1997) J Comput Chem , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.J.C.3
  • 35
    • 33846823909 scopus 로고
    • Particle Mesh Ewald - An N.Log(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L. Particle Mesh Ewald - an N.Log(N) method for Ewald sums in large systems. J Chem Phys 1993 98 : 10089 10092.
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 36
    • 0033556236 scopus 로고    scopus 로고
    • Peptide folding: When simulation meets experiment
    • Daura X, Gademann K, Jaun B et al. Peptide folding: when simulation meets experiment. Angew Chem Int Ed Engl 1999 38 : 236 240.
    • (1999) Angew Chem Int Ed Engl , vol.38 , pp. 236-240
    • Daura, X.1    Gademann, K.2    Jaun, B.3
  • 37
    • 9144232229 scopus 로고    scopus 로고
    • Molecular pharmacology of the ovine melatonin receptor: Comparison with recombinant human MT1 and MT2 receptors
    • Mailliet F, Audinot V, Malpaux B et al. Molecular pharmacology of the ovine melatonin receptor: comparison with recombinant human MT1 and MT2 receptors. Biochem Pharmacol 2004 67 : 667 677.
    • (2004) Biochem Pharmacol , vol.67 , pp. 667-677
    • Mailliet, F.1    Audinot, V.2    Malpaux, B.3
  • 38
    • 0034948696 scopus 로고    scopus 로고
    • Structural mimicry in G protein-coupled receptors: Implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors
    • Ballesteros JA, Shi L, Javitch JA. Structural mimicry in G protein-coupled receptors: implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors. Mol Pharmacol 2001 60 : 1 19.
    • (2001) Mol Pharmacol , vol.60 , pp. 1-19
    • Ballesteros, J.A.1    Shi, L.2    Javitch, J.A.3
  • 39
    • 0032546596 scopus 로고    scopus 로고
    • Spectroscopic evidence for interaction between transmembrane helices 3 and 5 in rhodopsin
    • Beck M, Sakmar TP, Siebert F. Spectroscopic evidence for interaction between transmembrane helices 3 and 5 in rhodopsin. Biochemistry 1998 37 : 7630 7639.
    • (1998) Biochemistry , vol.37 , pp. 7630-7639
    • Beck, M.1    Sakmar, T.P.2    Siebert, F.3
  • 40
    • 0028793627 scopus 로고
    • The conserved seven-transmembrane sequence NP(X)2,3Y of the G-protein-coupled receptor superfamily regulates multiple properties of the beta 2-adrenergic receptor
    • Barak LS, Menard L, Ferguson SS et al. The conserved seven-transmembrane sequence NP(X)2,3Y of the G-protein-coupled receptor superfamily regulates multiple properties of the beta 2-adrenergic receptor. Biochemistry 1995 34 : 15407 15414.
    • (1995) Biochemistry , vol.34 , pp. 15407-15414
    • Barak, L.S.1    Menard, L.2    Ferguson, S.S.3
  • 41
    • 0030922145 scopus 로고    scopus 로고
    • Interactions between conserved residues in transmembrane helices 1, 2, and 7 of the thyrotropin-releasing hormone receptor
    • Perlman JH, Colson AO, Wang W et al. Interactions between conserved residues in transmembrane helices 1, 2, and 7 of the thyrotropin-releasing hormone receptor. J Biol Chem 1997 272 : 11937 11942.
    • (1997) J Biol Chem , vol.272 , pp. 11937-11942
    • Perlman, J.H.1    Colson, A.O.2    Wang, W.3
  • 42
    • 0035823524 scopus 로고    scopus 로고
    • Transmembrane domains 4 and 7 of the M(1) muscarinic acetylcholine receptor are critical for ligand binding and the receptor activation switch
    • Lu ZL, Saldanha JW, Hulme EC. Transmembrane domains 4 and 7 of the M(1) muscarinic acetylcholine receptor are critical for ligand binding and the receptor activation switch. J Biol Chem 2001 276 : 34098 34104.
    • (2001) J Biol Chem , vol.276 , pp. 34098-34104
    • Lu, Z.L.1    Saldanha, J.W.2    Hulme, E.C.3
  • 43
    • 0344406765 scopus 로고    scopus 로고
    • Role of the conserved NPxxY(x)5,6F motif in the rhodopsin ground state and during activation
    • Fritze O, Filipek S, Kuksa V et al. Role of the conserved NPxxY(x)5,6F motif in the rhodopsin ground state and during activation. Proc Natl Acad Sci U S A 2003 100 : 2290 2295.
    • (2003) Proc Natl Acad Sci U S a , vol.100 , pp. 2290-2295
    • Fritze, O.1    Filipek, S.2    Kuksa, V.3
  • 44
    • 3843130785 scopus 로고    scopus 로고
    • Mutation of tyrosine in the conserved NPXXY sequence leads to constitutive phosphorylation and internalization, but not signaling, of the human B2 bradykinin receptor
    • Kalatskaya I, Schussler S, Blaukat A et al. Mutation of tyrosine in the conserved NPXXY sequence leads to constitutive phosphorylation and internalization, but not signaling, of the human B2 bradykinin receptor. J Biol Chem 2004 279 : 31268 31276.
    • (2004) J Biol Chem , vol.279 , pp. 31268-31276
    • Kalatskaya, I.1    Schussler, S.2    Blaukat, A.3
  • 45
    • 0032541084 scopus 로고    scopus 로고
    • G protein-coupled receptors. II. Mechanism of agonist activation
    • Gether U, Kobilka BK. G protein-coupled receptors. II. Mechanism of agonist activation. J Biol Chem 1998 273 : 17979 17982.
    • (1998) J Biol Chem , vol.273 , pp. 17979-17982
    • Gether, U.1    Kobilka, B.K.2
  • 46
    • 0029778268 scopus 로고    scopus 로고
    • Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F
    • Sheikh SP, Zvyaga TA, Lichtarge O et al. Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F. Nature 1996 383 : 347 350.
    • (1996) Nature , vol.383 , pp. 347-350
    • Sheikh, S.P.1    Zvyaga, T.A.2    Lichtarge, O.3
  • 47
    • 0037197848 scopus 로고    scopus 로고
    • Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography
    • Okada T, Fujiyoshi Y, Silow M et al. Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography. Proc Natl Acad Sci U S A 2002 99 : 5982 5987.
    • (2002) Proc Natl Acad Sci U S a , vol.99 , pp. 5982-5987
    • Okada, T.1    Fujiyoshi, Y.2    Silow, M.3
  • 48
    • 0030201178 scopus 로고    scopus 로고
    • The high affinity melationin binding site probed with conformationally restricted ligand - I. Pharmacophore and minireceptor models
    • Jansen JM, Copinga S, Gruppen G et al. The high affinity melationin binding site probed with conformationally restricted ligand - I. Pharmacophore and minireceptor models. Bioorg Med Chem 1996 4 : 1321 1332.
    • (1996) Bioorg Med Chem , vol.4 , pp. 1321-1332
    • Jansen, J.M.1    Copinga, S.2    Gruppen, G.3
  • 49
    • 1542379652 scopus 로고    scopus 로고
    • Evolutionary trace of G protein-coupled receptors reveals clusters of residues that determine global and class-specific functions
    • Madabushi S, Gross AK, Philippi A et al. Evolutionary trace of G protein-coupled receptors reveals clusters of residues that determine global and class-specific functions. J Biol Chem 2004 279 : 8126 8132.
    • (2004) J Biol Chem , vol.279 , pp. 8126-8132
    • Madabushi, S.1    Gross, A.K.2    Philippi, A.3
  • 50
    • 0038771257 scopus 로고    scopus 로고
    • Mutagenesis studies of the human MT2 melatonin receptor
    • Gerdin MJ, Mseeh F, Dubocovich ML. Mutagenesis studies of the human MT2 melatonin receptor. Biochem Pharmacol 2003 66 : 315 320.
    • (2003) Biochem Pharmacol , vol.66 , pp. 315-320
    • Gerdin, M.J.1    Mseeh, F.2    Dubocovich, M.L.3
  • 51
    • 33745224117 scopus 로고    scopus 로고
    • Metal ion site engineering indicates a global toggle switch model for seven-transmembrane receptor activation
    • Elling CE, Frimurer TM, Gerlach LO et al. Metal ion site engineering indicates a global toggle switch model for seven-transmembrane receptor activation. J Biol Chem 2006 281 : 17337 17346.
    • (2006) J Biol Chem , vol.281 , pp. 17337-17346
    • Elling, C.E.1    Frimurer, T.M.2    Gerlach, L.O.3
  • 52
    • 0029964709 scopus 로고    scopus 로고
    • Identification of amino acid residues in transmembrane helices VI and VII of the lutropin/choriogonadotropin receptor involved in signaling
    • Fernandez LM, Puett D. Identification of amino acid residues in transmembrane helices VI and VII of the lutropin/choriogonadotropin receptor involved in signaling. Biochemistry 1996 35 : 3986 3993.
    • (1996) Biochemistry , vol.35 , pp. 3986-3993
    • Fernandez, L.M.1    Puett, D.2
  • 53
    • 0035798651 scopus 로고    scopus 로고
    • Control of conformational equilibria in the human B2 bradykinin receptor. Modeling of nonpeptidic ligand action and comparison to the rhodopsin structure
    • Marie J, Richard E, Pruneau D et al. Control of conformational equilibria in the human B2 bradykinin receptor. Modeling of nonpeptidic ligand action and comparison to the rhodopsin structure. J Biol Chem 2001 276 : 41100 41111.
    • (2001) J Biol Chem , vol.276 , pp. 41100-41111
    • Marie, J.1    Richard, E.2    Pruneau, D.3
  • 54
    • 0038741910 scopus 로고    scopus 로고
    • Important amino acids for the function of the human MT1 melatonin receptor
    • Kokkola T, Foord SM, Watson MA et al. Important amino acids for the function of the human MT1 melatonin receptor. Biochem Pharmacol 2003 65 : 1463 1471.
    • (2003) Biochem Pharmacol , vol.65 , pp. 1463-1471
    • Kokkola, T.1    Foord, S.M.2    Watson, M.A.3
  • 55
    • 0031581101 scopus 로고    scopus 로고
    • The roles of valine 208 and histidine 211 in ligand binding and receptor function of the ovine Mel1a beta melatonin receptor
    • Conway S, Canning SJ, Barrett P et al. The roles of valine 208 and histidine 211 in ligand binding and receptor function of the ovine Mel1a beta melatonin receptor. Biochem Biophys Res Commun 1997 239 : 418 423.
    • (1997) Biochem Biophys Res Commun , vol.239 , pp. 418-423
    • Conway, S.1    Canning, S.J.2    Barrett, P.3
  • 56
    • 19744373593 scopus 로고    scopus 로고
    • Ligand binding to the human MT2 melatonin receptor: The role of residues in transmembrane domains 3, 6, and 7
    • Mazna P, Berka K, Jelinkova I et al. Ligand binding to the human MT2 melatonin receptor: the role of residues in transmembrane domains 3, 6, and 7. Biochem Biophys Res Commun 2005 332 : 726 734.
    • (2005) Biochem Biophys Res Commun , vol.332 , pp. 726-734
    • Mazna, P.1    Berka, K.2    Jelinkova, I.3
  • 57
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones DT. Protein secondary structure prediction based on position-specific scoring matrices. J Mol Biol 1999 292 : 195 202.
    • (1999) J Mol Biol , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 58
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • Mcguffin LJ, Bryson K, Jones DT. The PSIPRED protein structure prediction server. Bioinformatics 2000 16 : 404 405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.