메뉴 건너뛰기




Volumn 13, Issue 8, 2004, Pages 1997-2008

Modeling and simulation of the human δ opioid receptor

Author keywords

Activation mechanism; Agonist antagonist binding; Bovine rhodopsin; GPCR; Molecular dynamics

Indexed keywords

OPIATE AGONIST; OPIATE ANTAGONIST; RHODOPSIN; SIGMA OPIATE RECEPTOR;

EID: 3342939776     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.04720304     Document Type: Article
Times cited : (26)

References (103)
  • 1
    • 0029815140 scopus 로고    scopus 로고
    • Modulation of GDP release from transducin by the conserved Glu134-Arg135 sequence in rhodopsin
    • Acharya, S. and Karnik, S.S. 1996. Modulation of GDP release from transducin by the conserved Glu134-Arg135 sequence in rhodopsin. J. Biol. Chem. 271: 25406-25411.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25406-25411
    • Acharya, S.1    Karnik, S.S.2
  • 3
    • 0034112037 scopus 로고    scopus 로고
    • The effect of mutations in the DRY motif on the constitutive activity and structural instability of the histamine H2 receptor
    • Alewijnse, A.E., Timmerman, H., Jacobs, E.H., Smit, M.J., Roovers, E., Cotecchia, S., and Leurs, R. 2000. The effect of mutations in the DRY motif on the constitutive activity and structural instability of the histamine H2 receptor. Mol. Pharmacol. 57: 890-898.
    • (2000) Mol. Pharmacol. , vol.57 , pp. 890-898
    • Alewijnse, A.E.1    Timmerman, H.2    Jacobs, E.H.3    Smit, M.J.4    Roovers, E.5    Cotecchia, S.6    Leurs, R.7
  • 4
    • 0029947902 scopus 로고    scopus 로고
    • A 3D model of the δ opioid receptor and ligand-receptor complexes
    • Alkorta, I. and Loew, G.H. 1996. A 3D model of the δ opioid receptor and ligand-receptor complexes. Protein Eng. 9: 573-583.
    • (1996) Protein Eng. , vol.9 , pp. 573-583
    • Alkorta, I.1    Loew, G.H.2
  • 5
    • 0028061193 scopus 로고
    • A conserved carboxylic acid group mediates light-dependent proton uptake and signaling by rhodopsin
    • Arnis, S., Fahmy, K., Hofmann, K.P., and Sakmar, T.P. 1994. A conserved carboxylic acid group mediates light-dependent proton uptake and signaling by rhodopsin. J. Biol. Chem. 269: 23879-23881.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23879-23881
    • Arnis, S.1    Fahmy, K.2    Hofmann, K.P.3    Sakmar, T.P.4
  • 6
    • 0027506471 scopus 로고
    • The probable arrangement of the helices in G protein-coupled receptors
    • Baldwin, J.M. 1993. The probable arrangement of the helices in G protein-coupled receptors. EMBO J. 12: 1693-1703.
    • (1993) EMBO J. , vol.12 , pp. 1693-1703
    • Baldwin, J.M.1
  • 7
    • 0031565726 scopus 로고    scopus 로고
    • An α-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors
    • Baldwin, J.M., Schertler, G.F.X., and Unger, V.M. 1997. An α-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.X.2    Unger, V.M.3
  • 8
    • 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, J.A. and Weinstein, H. 1995. Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptors. Meth. Neurosci. 25: 365-428.
    • (1995) Meth. Neurosci. , vol.25 , pp. 365-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 10
    • 0029937609 scopus 로고    scopus 로고
    • Role of aromatic transmembrane residues of the δ opioid receptor in ligand recognition
    • Befort, K., Tabbara, D.K., Maigret, B., and Kieffer, B.L. 1996a. Role of aromatic transmembrane residues of the δ opioid receptor in ligand recognition. J. Biol. Chem. 271: 10161-10168.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10161-10168
    • Befort, K.1    Tabbara, D.K.2    Maigret, B.3    Kieffer, B.L.4
  • 11
    • 0030040907 scopus 로고    scopus 로고
    • The conserved aspartate residue in the third putative transmembrane domain of the δ opioid receptor is not the anionic counterpart for cationic opiate binding but is a constituent of the receptor binding site
    • Befort, K., Tabbara, L., Bausch, S., Chavkin, C., Evans, C., and Kieffer, B.L. 1996b. The conserved aspartate residue in the third putative transmembrane domain of the δ opioid receptor is not the anionic counterpart for cationic opiate binding but is a constituent of the receptor binding site. Mol. Pharmacol. 49: 216-223.
    • (1996) Mol. Pharmacol. , vol.49 , pp. 216-223
    • Befort, K.1    Tabbara, L.2    Bausch, S.3    Chavkin, C.4    Evans, C.5    Kieffer, B.L.6
  • 12
    • 0033603318 scopus 로고    scopus 로고
    • Constitutive activation of the δ opioid receptor by mutations in transmembrane domains III and VII
    • Befort, K., Zilliox, C., Filliol, D., Yue, S.Y., and Kieffer, B.L. 1999. Constitutive activation of the δ opioid receptor by mutations in transmembrane domains III and VII. J. Biol. Chem. 274: 18574-18581.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18574-18581
    • Befort, K.1    Zilliox, C.2    Filliol, D.3    Yue, S.Y.4    Kieffer, B.L.5
  • 13
    • 0002775934 scopus 로고
    • Interaction models for water in relation to protein hydration
    • (ed. B. Pullman). D. Reidel Publishing, Dordrecht, The Netherlands
    • Berendsen, H.J.C., Postma, J.P.M., van Gunsteren, W.F., and Hermans, J. 1981. Interaction models for water in relation to protein hydration. In Intermolecular forces (ed. B. Pullman), pp. 331-342. D. Reidel Publishing, Dordrecht, The Netherlands.
    • (1981) Intermolecular Forces , pp. 331-342
    • Berendsen, H.J.C.1    Postma, J.P.M.2    Van Gunsteren, W.F.3    Hermans, J.4
  • 15
    • 0242362716 scopus 로고    scopus 로고
    • Conformational changes of G-protein coupled receptors during their activation by agonist binding
    • Bissantz, C. 2003. Conformational changes of G-protein coupled receptors during their activation by agonist binding. J. Recept. Signal Trans. 23: 123-153.
    • (2003) J. Recept. Signal Trans. , vol.23 , pp. 123-153
    • Bissantz, C.1
  • 16
    • 0037235663 scopus 로고    scopus 로고
    • Protein-based virtual screening of chemical databases. II: Are homology models of G-protein coupled receptors suitable targets?
    • Bissantz, C., Bernard, P., Hilbert, M., and Rognan, D. 2003. Protein-based virtual screening of chemical databases, II: Are homology models of G-protein coupled receptors suitable targets? Proteins 50: 5-25.
    • (2003) Proteins , vol.50 , pp. 5-25
    • Bissantz, C.1    Bernard, P.2    Hilbert, M.3    Rognan, D.4
  • 18
    • 0033118238 scopus 로고    scopus 로고
    • A molecular mechanism for the cleavage of a disulfide bond as the primary function of agonist binding to G-protein coupled receptors based on theoretical calculations supported by experiments
    • Brandt, W., Golbraikh, A., Tager, M., and Lendeckel, U. 1999. A molecular mechanism for the cleavage of a disulfide bond as the primary function of agonist binding to G-protein coupled receptors based on theoretical calculations supported by experiments. Eur. J. Biochem. 261: 89-97.
    • (1999) Eur. J. Biochem. , vol.261 , pp. 89-97
    • Brandt, W.1    Golbraikh, A.2    Tager, M.3    Lendeckel, U.4
  • 19
    • 0346059583 scopus 로고    scopus 로고
    • G protein-coupled receptor oligomerisation
    • Breitwieser, G.E. 2004. G protein-coupled receptor oligomerisation. Circ. Res. 94: 17-27.
    • (2004) Circ. Res. , vol.94 , pp. 17-27
    • Breitwieser, G.E.1
  • 20
    • 0032544633 scopus 로고    scopus 로고
    • The second intracellular loop of the m5 muscarinic receptor is the switch which enables G-protein coupling
    • Burstein, E.S., Spalding, T.A., and Brann, M.R. 1998. The second intracellular loop of the m5 muscarinic receptor is the switch which enables G-protein coupling. J. Biol. Chem. 273: 24322-24327.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24322-24327
    • Burstein, E.S.1    Spalding, T.A.2    Brann, M.R.3
  • 21
    • 0021942907 scopus 로고
    • Trigger and amplification mechanism in visual phototransduction
    • Chabre, M. 1985. Trigger and amplification mechanism in visual phototransduction. Ann. Rev. Biophys. Biophys. Chem. 14: 331-360.
    • (1985) Ann. Rev. Biophys. Biophys. Chem. , vol.14 , pp. 331-360
    • Chabre, M.1
  • 22
    • 0142179224 scopus 로고    scopus 로고
    • The first and third intracellular loops together with carboxy terminal tail of the δ opioid receptor contribute toward functional interaction with G α16
    • Chan, A.S.L., Law, P.Y., Loh, H.H., Ho, P.N.N., Wu, W., Chan, J.S.C., and Wong, Y.H. 2003. The first and third intracellular loops together with carboxy terminal tail of the δ opioid receptor contribute toward functional interaction with G α16. J. Neurochem. 87: 697-708.
    • (2003) J. Neurochem. , vol.87 , pp. 697-708
    • Chan, A.S.L.1    Law, P.Y.2    Loh, H.H.3    Ho, P.N.N.4    Wu, W.5    Chan, J.S.C.6    Wong, Y.H.7
  • 23
    • 0030175693 scopus 로고    scopus 로고
    • Characterization of the bioactive form of linear antagonists at the ω-opioid receptor
    • Chao, T.M., Perez, J.J., and Loew, G.H. 1996. Characterization of the bioactive form of linear antagonists at the ω-opioid receptor. Biopolymers 38: 759-768.
    • (1996) Biopolymers , vol.38 , pp. 759-768
    • Chao, T.M.1    Perez, J.J.2    Loew, G.H.3
  • 25
    • 0027202213 scopus 로고
    • Molecular cloning and functional expression of a m-opioid receptor from rat brain
    • Chen, Y., Mestek, A., Liu, J., Hurley, J.A., and Yu, L. 1993. Molecular cloning and functional expression of a m-opioid receptor from rat brain. Mol. Pharmacol. 44: 8-12.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 8-12
    • Chen, Y.1    Mestek, A.2    Liu, J.3    Hurley, J.A.4    Yu, L.5
  • 26
    • 0036258990 scopus 로고    scopus 로고
    • G protein-coupled receptor allosterism and complexing
    • Christopoulos, A. and Kenakin, T. 2002. G protein-coupled receptor allosterism and complexing. Pharmacol. Rev. 54: 323-374.
    • (2002) Pharmacol. Rev. , vol.54 , pp. 323-374
    • Christopoulos, A.1    Kenakin, T.2
  • 27
    • 0030760634 scopus 로고    scopus 로고
    • Dimerization of the δ opioid receptor: Implication for a role in receptor internalization
    • Cvejic, S. and Devi, L.A. 1997. Dimerization of the δ opioid receptor: Implication for a role in receptor internalization. J. Biol. Chem. 272: 26959-26964.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26959-26964
    • Cvejic, S.1    Devi, L.A.2
  • 28
    • 0042624659 scopus 로고    scopus 로고
    • Opioid receptor random mutagenesis reveals a mechanism for G protein-coupled receptor activation
    • Decaillot, F.M., Befort, K., Filliol, D., Yue, S., Walker, P., and Kieffer, B.L. 2003. Opioid receptor random mutagenesis reveals a mechanism for G protein-coupled receptor activation. Nat. Struct. Biol. 10: 629-636.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 629-636
    • Decaillot, F.M.1    Befort, K.2    Filliol, D.3    Yue, S.4    Walker, P.5    Kieffer, B.L.6
  • 30
    • 0035700627 scopus 로고    scopus 로고
    • Heterotrimeric G-proteins and their role in opioid receptor function
    • Fabian, G. 2001. Heterotrimeric G-proteins and their role in opioid receptor function. Acta Biologica Szegediensis 45: 13-21.
    • (2001) Acta Biologica Szegediensis , vol.45 , pp. 13-21
    • Fabian, G.1
  • 31
    • 0347994106 scopus 로고    scopus 로고
    • Refinement of homology-based protein structures by molecular dynamics simulation techniques
    • Fan, H. and Mark, A.E. 2004. Refinement of homology-based protein structures by molecular dynamics simulation techniques. Protein Sci. 13: 211-220.
    • (2004) Protein Sci. , vol.13 , pp. 211-220
    • Fan, H.1    Mark, A.E.2
  • 32
    • 0037671392 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the bacterial outer membrane protein fluA: A comparative study of the ferrichrome-free and bound states
    • Faraldo-Gomez, J.D., Smith, G.R., and Sansom, M.S.P. 2003. Molecular dynamics simulations of the bacterial outer membrane protein fluA: A comparative study of the ferrichrome-free and bound states. Biophys. J. 85: 1406-1420.
    • (2003) Biophys. J. , vol.85 , pp. 1406-1420
    • Faraldo-Gomez, J.D.1    Smith, G.R.2    Sansom, M.S.P.3
  • 33
    • 0001278467 scopus 로고
    • The opiate receptor: A model explaining structure-activity relationships of agonists and antagonists
    • Feinberg, A.P., Creese, I., and Synder, S.H. 1976. The opiate receptor: A model explaining structure-activity relationships of agonists and antagonists. Proc. Natl. Acad. Sci. 73: 4215-4219.
    • (1976) Proc. Natl. Acad. Sci. , vol.73 , pp. 4215-4219
    • Feinberg, A.P.1    Creese, I.2    Synder, S.H.3
  • 34
    • 0032808048 scopus 로고    scopus 로고
    • Molecular modeling study of the differential ligand-receptor interaction at the μ, δ and κ opioid receptors
    • Filizola, M., Carteni-Farina, M., and Perez, J.B. 1999a. Molecular modeling study of the differential ligand-receptor interaction at the μ, δ and κ opioid receptors. J. Comput. Aided Mol. Design 13: 397-407.
    • (1999) J. Comput. Aided Mol. Design. , vol.13 , pp. 397-407
    • Filizola, M.1    Carteni-Farina, M.2    Perez, J.B.3
  • 35
    • 0032709594 scopus 로고    scopus 로고
    • Three-dimensional modeling, ligand binding and activation studies of the cloned mouse δ, μ and κ opioid receptors
    • Filizola, M., Laakkonen, L., and Loew, G.H. 1999b. Three-dimensional modeling, ligand binding and activation studies of the cloned mouse δ, μ and κ opioid receptors. Protein Eng. 12: 927-942.
    • (1999) Protein Eng. , vol.12 , pp. 927-942
    • Filizola, M.1    Laakkonen, L.2    Loew, G.H.3
  • 36
    • 0035185186 scopus 로고    scopus 로고
    • Molecular determinants of nonspecific recognition of δ, μ and κ opioid receptors
    • Filizola, M., Villar, H.O., and Loew, G.H. 2001. Molecular determinants of nonspecific recognition of δ, μ and κ opioid receptors. Bioorg. Med. Chem. 9: 69-76.
    • (2001) Bioorg. Med. Chem. , vol.9 , pp. 69-76
    • Filizola, M.1    Villar, H.O.2    Loew, G.H.3
  • 37
    • 0028934926 scopus 로고
    • Location of regions of the opioid receptor involved in selective agonist binding
    • Fukuda, K., Kato, S., and Mori, K. 1995. Location of regions of the opioid receptor involved in selective agonist binding. J. Biol. Chem. 270: 6702-6709.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6702-6709
    • Fukuda, K.1    Kato, S.2    Mori, K.3
  • 39
    • 0034464742 scopus 로고    scopus 로고
    • Uncovering molecular mechanisms involved in activation of G protein-coupled receptors
    • Gether, U. 2000. Uncovering molecular mechanisms involved in activation of G protein-coupled receptors. Endocrine Rev. 21: 90-113.
    • (2000) Endocrine Rev. , vol.21 , pp. 90-113
    • Gether, U.1
  • 42
    • 0032856161 scopus 로고    scopus 로고
    • Buried, charged, non-ion-paired aspartic acid 76 contributes favorably to the conformational stability of ribonuclease T1
    • Giletto, A. and Pace, N. 1999. Buried, charged, non-ion-paired aspartic acid 76 contributes favorably to the conformational stability of ribonuclease T1. Biochemistry 38: 13379-13384.
    • (1999) Biochemistry , vol.38 , pp. 13379-13384
    • Giletto, A.1    Pace, N.2
  • 43
    • 0023062991 scopus 로고
    • G proteins: Transducers or receptor-generated signals
    • Gilman, A.G. 1987. G proteins: Transducers or receptor-generated signals. Ann. Rev. Biochem. 56: 615-649.
    • (1987) Ann. Rev. Biochem. , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 44
    • 0024696696 scopus 로고
    • Evidence for the presence of disulfide bridges in opioid receptors essential for ligand binding: Possible role in receptor activation
    • Gioannini, T.L., Liu, Y.F., Park, Y.H., Hiller, J.M., and Simon, E.J. 1989. Evidence for the presence of disulfide bridges in opioid receptors essential for ligand binding: Possible role in receptor activation. J. Mol. Recog. 2: 44-48.
    • (1989) J. Mol. Recog. , vol.2 , pp. 44-48
    • Gioannini, T.L.1    Liu, Y.F.2    Park, Y.H.3    Hiller, J.M.4    Simon, E.J.5
  • 45
  • 46
    • 0025292355 scopus 로고
    • An atomic model for the structure of bacteriorhodopsin
    • Henderson, R., Baldwin, J.M., and Ceska, T.A. 1990. An atomic model for the structure of bacteriorhodopsin. J. Mol. Biol. 213: 899-929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3
  • 47
    • 0034563322 scopus 로고    scopus 로고
    • Receptor coupling to G proteins: Is there a signal behind the sequence?
    • Horn, F., van der Wenden, E.M., Oliveira, L., IJzerman, A.P., and Vriend, G. 2000. Receptor coupling to G proteins: Is there a signal behind the sequence? Proteins 41: 448-459.
    • (2000) Proteins , vol.41 , pp. 448-459
    • Horn, F.1    Van Der Wenden, E.M.2    Oliveira, L.3    Ijzerman, A.P.4    Vriend, G.5
  • 50
    • 0037168078 scopus 로고    scopus 로고
    • κ-opioid receptor model in a phospholipid bilayer: Molecular dynamics simulations
    • Iadanza, M., Holtje, M., Ronsisvalle, G., and Holtje, H.D. 2002. κ-opioid receptor model in a phospholipid bilayer: Molecular dynamics simulations. J. Med. Chem. 45: 4843-4846.
    • (2002) J. Med. Chem. , vol.45 , pp. 4843-4846
    • Iadanza, M.1    Holtje, M.2    Ronsisvalle, G.3    Holtje, H.D.4
  • 51
    • 0032504237 scopus 로고    scopus 로고
    • G protein-coupled receptors. I: Diversity of receptor-ligand interactions
    • Ji, T.H., Grossmann, M., and Ji, I. 1998. G protein-coupled receptors, I: Diversity of receptor-ligand interactions. J. Biol. Chem. 273: 17299-17302.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17299-17302
    • Ji, T.H.1    Grossmann, M.2    Ji, I.3
  • 53
    • 0027052952 scopus 로고
    • The δ-opioid receptor: Isolation of a cDNA by expression cloning and pharmacological characterization
    • Kieffer, B.L., Befort, K., Gaveriaux-Ruff, C., and Hirth, C.G. 1992. The δ-opioid receptor: Isolation of a cDNA by expression cloning and pharmacological characterization. Proc. Natl. Acad. Sci. 89: 12048-12052.
    • (1992) Proc. Natl. Acad. Sci. , vol.89 , pp. 12048-12052
    • Kieffer, B.L.1    Befort, K.2    Gaveriaux-Ruff, C.3    Hirth, C.G.4
  • 54
    • 0027444691 scopus 로고
    • A single residue, aspartic acid 95, in the δ opioid receptor specifies selective high affinity agonist binding
    • Kong, H., Raynor, K., Yasuda, K., Moe, S.T., Portoghese, P.S., Bell, G.I., and Reisine, T. 1993. A single residue, aspartic acid 95, in the δ opioid receptor specifies selective high affinity agonist binding. J. Biol. Chem. 268: 23055-23058.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23055-23058
    • Kong, H.1    Raynor, K.2    Yasuda, K.3    Moe, S.T.4    Portoghese, P.S.5    Bell, G.I.6    Reisine, T.7
  • 55
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the steriochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Mass, D.S., and Thornton, J.M. 1993. PROCHECK: A program to check the steriochemical quality of protein structures. J. Appl. Crystallogr. 26: 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Mass, D.S.3    Thornton, J.M.4
  • 56
    • 0037434740 scopus 로고    scopus 로고
    • The effects of internal water molecules on the structure and dynamics of chymotrypsin inhibitor 2
    • Lei, H. and Smith, P.E. 2003. The effects of internal water molecules on the structure and dynamics of chymotrypsin inhibitor 2. J. Phys. Chem. B 107: 1395-1402.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 1395-1402
    • Lei, H.1    Smith, P.E.2
  • 58
    • 0031037632 scopus 로고    scopus 로고
    • The role of aspartate-arginine-tyrosine triad in the m1 muscarinic receptor: Mutations of aspartate 122 and tyrosine 124 decrease receptor expression but not abolish signalling
    • Lu, Z., Curtis, C.A., Jones, P.G., Pavia, J., and Hulme, E. 1997. The role of aspartate-arginine-tyrosine triad in the m1 muscarinic receptor: Mutations of aspartate 122 and tyrosine 124 decrease receptor expression but not abolish signalling. Mol. Pharmacol. 51: 234-241.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 234-241
    • Lu, Z.1    Curtis, C.A.2    Jones, P.G.3    Pavia, J.4    Hulme, E.5
  • 61
  • 62
    • 0028866118 scopus 로고
    • On the role of extracellular loops of opioid receptor in conferring ligand selectivity
    • Metzer, T. and Ferguson, D.M. 1995. On the role of extracellular loops of opioid receptor in conferring ligand selectivity. FEBS Lett. 375: 1-4.
    • (1995) FEBS Lett. , vol.375 , pp. 1-4
    • Metzer, T.1    Ferguson, D.M.2
  • 64
    • 0033511768 scopus 로고    scopus 로고
    • Complementarity of δ opioid ligand pharmacophore and receptor models
    • Mosberg, H.I. 1999. Complementarity of δ opioid ligand pharmacophore and receptor models. Biopolymers 51: 426-439.
    • (1999) Biopolymers , vol.51 , pp. 426-439
    • Mosberg, H.I.1
  • 65
    • 0028342488 scopus 로고
    • A statistical analysis of side-chain conformations in proteins: Comparison with ECEPP predictions
    • Nayeem, A. and Scheraga, H.A. 1994. A statistical analysis of side-chain conformations in proteins: Comparison with ECEPP predictions. J. Protein Chem. 13: 283-296.
    • (1994) J. Protein Chem. , vol.13 , pp. 283-296
    • Nayeem, A.1    Scheraga, H.A.2
  • 67
    • 1842335688 scopus 로고    scopus 로고
    • Novel "restoration of function" mutagenesis strategy to identify amino acids of the δ opioid receptor involved in ligand binding
    • Pepin, M., Yue, S.Y., Roberts, E., Wahlestedt, C., and Walker, P. 1997. Novel "restoration of function" mutagenesis strategy to identify amino acids of the δ opioid receptor involved in ligand binding. J. Biol. Chem. 272: 9260-9267.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9260-9267
    • Pepin, M.1    Yue, S.Y.2    Roberts, E.3    Wahlestedt, C.4    Walker, P.5
  • 68
    • 0031848224 scopus 로고    scopus 로고
    • Opioid receptor three-dimensional structures from distance geometry calculations with hydrogen bonding constraints
    • Pogozheva, I.D., Lomize, A.L., and Mosberg, H.I. 1998. Opioid receptor three-dimensional structures from distance geometry calculations with hydrogen bonding constraints. Biophysical J. 75: 612-634.
    • (1998) Biophysical J. , vol.75 , pp. 612-634
    • Pogozheva, I.D.1    Lomize, A.L.2    Mosberg, H.I.3
  • 69
    • 0025314942 scopus 로고
    • Design of peptidomimetic δ opioid receptor antagonists using the message-address concept
    • Portoghese, P.S., Sultana, M., and Takemori, A.E. 1990. Design of peptidomimetic δ opioid receptor antagonists using the message-address concept. J. Med. Chem. 33: 1714-1720.
    • (1990) J. Med. Chem. , vol.33 , pp. 1714-1720
    • Portoghese, P.S.1    Sultana, M.2    Takemori, A.E.3
  • 71
    • 0025960130 scopus 로고
    • Development of δ opioid peptides as non-addicting analgesics
    • Rapaka, R.S. and Porreca, F. 1991. Development of δ opioid peptides as non-addicting analgesics. Pharmacol. Res. 8: 1-8.
    • (1991) Pharmacol. Res. , vol.8 , pp. 1-8
    • Rapaka, R.S.1    Porreca, F.2
  • 72
    • 0033061256 scopus 로고    scopus 로고
    • Mutation of a highly conserved aspartic acid in the β2 adrenergic receptor: Constitutive activation, structural instability, and conformational rearrangement of transmembrane segment 6
    • Rasmussen, S.G.F., Jensen, A.D., Liapakis, G., Ghanouni, P., Javitch, J.A., and Gether, U. 1999. Mutation of a highly conserved aspartic acid in the β2 adrenergic receptor: Constitutive activation, structural instability, and conformational rearrangement of transmembrane segment 6. Mol. Pharmacol. 56: 175-184.
    • (1999) Mol. Pharmacol. , vol.56 , pp. 175-184
    • Rasmussen, S.G.F.1    Jensen, A.D.2    Liapakis, G.3    Ghanouni, P.4    Javitch, J.A.5    Gether, U.6
  • 74
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-Alkanes
    • Ryckaert, J.P., Ciccotti, G., and Berendsen, H.J.C. 1977. Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-Alkanes. J. Comput. Phys. 23: 327-341.
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 75
    • 0030880687 scopus 로고    scopus 로고
    • Evolution of the Dmt-Tic pharmacophore: N-terminal methylated derivatives with extraordinary δ opioid antagonist activity
    • Salvadori, S., Balboni, G., Guerrini, R., Tomatis, R., Bianchi, C., Bryant, S.D., Cooper, P.S., and Lazarus, L.H. 1997. Evolution of the Dmt-Tic pharmacophore: N-terminal methylated derivatives with extraordinary δ opioid antagonist activity. J. Med. Chem. 40: 3100-3108.
    • (1997) J. Med. Chem. , vol.40 , pp. 3100-3108
    • Salvadori, S.1    Balboni, G.2    Guerrini, R.3    Tomatis, R.4    Bianchi, C.5    Bryant, S.D.6    Cooper, P.S.7    Lazarus, L.H.8
  • 76
    • 0030614337 scopus 로고    scopus 로고
    • The activation process of the α1B-adrenergic receptor: Potential role of protonation and hydrophobicity of a highly conserved aspartate
    • Scheer, A., Fanelli, F., Costa, T., and De Benedetti, P.G. 1997. The activation process of the α1B-adrenergic receptor: Potential role of protonation and hydrophobicity of a highly conserved aspartate. Proc. Natl. Acad. Sci. 94: 808-813.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 808-813
    • Scheer, A.1    Fanelli, F.2    Costa, T.3    De Benedetti, P.G.4
  • 77
    • 0033974265 scopus 로고    scopus 로고
    • Mutational analysis of the highly conserved arginine within the Glu/Asp-Arg-Tyr motif of the α1b adrenergic receptor: Effects on receptor isomerisation and activation
    • Scheer, A., Costa, T., Fanelli, F., De Benedetti, P.G., Mhaouty-Kodja, S., Abuin, L., Nenniger-Tosata, M., and Cotecchia, S. 2000. Mutational analysis of the highly conserved arginine within the Glu/Asp-Arg-Tyr motif of the α1b adrenergic receptor: Effects on receptor isomerisation and activation. Mol. Pharmacol. 57: 219-231.
    • (2000) Mol. Pharmacol. , vol.57 , pp. 219-231
    • Scheer, A.1    Costa, T.2    Fanelli, F.3    De Benedetti, P.G.4    Mhaouty-Kodja, S.5    Abuin, L.6    Nenniger-Tosata, M.7    Cotecchia, S.8
  • 78
    • 0027190359 scopus 로고
    • Projection structure of rhodopsin
    • Schertler, G.F.X., Villa, C., and Henderson, R. 1993. Projection structure of rhodopsin. Nature 362: 770-772.
    • (1993) Nature , vol.362 , pp. 770-772
    • Schertler, G.F.X.1    Villa, C.2    Henderson, R.3
  • 79
    • 0027049066 scopus 로고
    • Differential stereochemical requirements of δ vs. μ opioid receptors for ligand binding and signal transduction: Development of a class of potent and highly δ-selective peptide antagonists
    • Schiller, P.W., Nguyen, T.M.D., Weltrowska, G., Wilkes, B.C., Marsden, B.J., Lemieux, C., and Chung, N.N. 1992. Differential stereochemical requirements of δ vs. μ opioid receptors for ligand binding and signal transduction: Development of a class of potent and highly δ-selective peptide antagonists. Proc. Natl. Acad. Sci. 89: 11871-11875.
    • (1992) Proc. Natl. Acad. Sci. , vol.89 , pp. 11871-11875
    • Schiller, P.W.1    Nguyen, T.M.D.2    Weltrowska, G.3    Wilkes, B.C.4    Marsden, B.J.5    Lemieux, C.6    Chung, N.N.7
  • 81
    • 0037835959 scopus 로고    scopus 로고
    • Conversion of δ, κ and μ receptor selective opioid peptide agonists into δ, κ and μ selective antagonists
    • Schiller, P.W., Weltrowska, G., Nguyen, T.M.D., Lemieux, C., Chung, N.N., and Lu, Y. 2003. Conversion of δ, κ and μ receptor selective opioid peptide agonists into δ, κ and μ selective antagonists. Life Sci. 73: 691-698.
    • (2003) Life Sci. , vol.73 , pp. 691-698
    • Schiller, P.W.1    Weltrowska, G.2    Nguyen, T.M.D.3    Lemieux, C.4    Chung, N.N.5    Lu, Y.6
  • 84
    • 0029863220 scopus 로고    scopus 로고
    • Studies on inhibition of μ and δ opioid receptor binding by dithiothreitol and N-ethylmaleimide
    • Shahrestanifar, M., Wang, W.W., and Howells, R.D. 1996. Studies on inhibition of μ and δ opioid receptor binding by dithiothreitol and N-ethylmaleimide. J. Biol. Chem. 271: 5505-5512.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5505-5512
    • Shahrestanifar, M.1    Wang, W.W.2    Howells, R.D.3
  • 85
    • 0034057869 scopus 로고    scopus 로고
    • A three-dimensional model of the δ opioid pharmacophore: Comparative molecular modeling of peptide and nonpeptide ligands
    • Shenderovich, M.D., Liao, S., Qian, X., and Hruby, V.J. 2000. A three-dimensional model of the δ opioid pharmacophore: Comparative molecular modeling of peptide and nonpeptide ligands. Biopolymers 53: 565-580.
    • (2000) Biopolymers , vol.53 , pp. 565-580
    • Shenderovich, M.D.1    Liao, S.2    Qian, X.3    Hruby, V.J.4
  • 86
    • 0024009898 scopus 로고
    • The molecular basis of opioid receptor function
    • Simonds, W.F. 1988. The molecular basis of opioid receptor function. Endocrine Rev. 9: 200-212.
    • (1988) Endocrine Rev. , vol.9 , pp. 200-212
    • Simonds, W.F.1
  • 87
    • 0018144087 scopus 로고
    • Conformation of leu enkephalin from X-ray diffraction: Features important for recognition at opiate receptor
    • Smith, D.G. and Griffin, J.F. 1978. Conformation of leu enkephalin from X-ray diffraction: Features important for recognition at opiate receptor. Science 199: 1214-1216.
    • (1978) Science , vol.199 , pp. 1214-1216
    • Smith, D.G.1    Griffin, J.F.2
  • 88
    • 0042243639 scopus 로고    scopus 로고
    • Opioid receptor interactions: Local and non-local symmetric and asymmetric, physical and functional
    • Smith, A.P. and Lee, N.M. 2003. Opioid receptor interactions: Local and non-local symmetric and asymmetric, physical and functional. Life Sci. 73: 1873-1893.
    • (2003) Life Sci. , vol.73 , pp. 1873-1893
    • Smith, A.P.1    Lee, N.M.2
  • 89
    • 2242491482 scopus 로고
    • Consistent dielectric properties of the simple point charge and extended simple point charge water models at 277 and 300K
    • Smith, P.E. and van Gunsteren, W.F. 1994. Consistent dielectric properties of the simple point charge and extended simple point charge water models at 277 and 300K. J. Chem. Phys. 100: 3169-3174.
    • (1994) J. Chem. Phys. , vol.100 , pp. 3169-3174
    • Smith, P.E.1    Van Gunsteren, W.F.2
  • 90
    • 0037020273 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G-protein-coupled receptor
    • Stenkamp, R.E., Teller, D.C., and Palczewski, K. 2002. Crystal structure of rhodopsin: A G-protein-coupled receptor. ChemBioChem 3: 963-967.
    • (2002) ChemBioChem , vol.3 , pp. 963-967
    • Stenkamp, R.E.1    Teller, D.C.2    Palczewski, K.3
  • 91
    • 0033783932 scopus 로고    scopus 로고
    • On the similarity of properties in solution or in the crystalline state: A molecular dynamics study of hen lysosome
    • Stocker, U., Spiegel, K., and van Gunsteren, W.F. 2000. On the similarity of properties in solution or in the crystalline state: A molecular dynamics study of hen lysosome. J. Biomol. NMR 18: 1-12.
    • (2000) J. Biomol. NMR , vol.18 , pp. 1-12
    • Stocker, U.1    Spiegel, K.2    Van Gunsteren, W.F.3
  • 93
    • 0031436823 scopus 로고    scopus 로고
    • Comparative modeling and molecular dynamics studies of the δ, κ and μ opioid receptors
    • Strahs, D. and Weinstein, H. 1997. Comparative modeling and molecular dynamics studies of the δ, κ and μ opioid receptors. Protein Eng. 10: 1019-1038.
    • (1997) Protein Eng. , vol.10 , pp. 1019-1038
    • Strahs, D.1    Weinstein, H.2
  • 94
    • 4544369164 scopus 로고
    • A generalized reaction field method for molecular dynamics simulations
    • Tironi, I.G., Sperb, R., Smith, P.E., and van Gunsteren, W.F. 1995. A generalized reaction field method for molecular dynamics simulations. J. Chem. Phys. 102: 5451-5459.
    • (1995) J. Chem. Phys. , vol.102 , pp. 5451-5459
    • Tironi, I.G.1    Sperb, R.2    Smith, P.E.3    Van Gunsteren, W.F.4
  • 96
    • 10144241052 scopus 로고    scopus 로고
    • Involvement of Trp-284, Val-296, Val-297 of the human δ opioid receptor in binding of δ selective ligands
    • Valiquette, M., Vu, H.K., Yue, S.Y., Wahlestedt, C., and Walker, P. 1996. Involvement of Trp-284, Val-296, Val-297 of the human δ opioid receptor in binding of δ selective ligands. J. Biol. Chem. 271: 18789-18796.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18789-18796
    • Valiquette, M.1    Vu, H.K.2    Yue, S.Y.3    Wahlestedt, C.4    Walker, P.5
  • 97
    • 0001349174 scopus 로고    scopus 로고
    • Validation of molecular dynamics simulations
    • van Gunsteren, W.F. and Mark, A.E. 1998. Validation of molecular dynamics simulations. J. Chem. Phys. 108: 6109-6116.
    • (1998) J. Chem. Phys. , vol.108 , pp. 6109-6116
    • Van Gunsteren, W.F.1    Mark, A.E.2
  • 98
    • 0034697979 scopus 로고    scopus 로고
    • Molecular dynamics simulations highlight mobile regions in proteins: A novel suggestion for converting a murine VH domain into a more tractable species
    • Voordijk, S., Hansson, T., Hilvert, D., and van Gunsteren, W.F. 2000. Molecular dynamics simulations highlight mobile regions in proteins: A novel suggestion for converting a murine VH domain into a more tractable species. J. Mol. Biol. 300: 963-973.
    • (2000) J. Mol. Biol. , vol.300 , pp. 963-973
    • Voordijk, S.1    Hansson, T.2    Hilvert, D.3    Van Gunsteren, W.F.4
  • 99
    • 0029564595 scopus 로고
    • Are buried salt bridges important for protein stability and conformational specificity?
    • Waldburger, C.D., Schildbach, J.F., and Sauer, R.T. 1995. Are buried salt bridges important for protein stability and conformational specificity? Nat. Struct. Biol. 2: 122-128.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 122-128
    • Waldburger, C.D.1    Schildbach, J.F.2    Sauer, R.T.3
  • 100
    • 0032402450 scopus 로고    scopus 로고
    • Molecular basis of receptor/G-protein-coupling selectivity
    • Wess, J. 1998. Molecular basis of receptor/G-protein-coupling selectivity. Pharmacol. Ther. 80: 231-264.
    • (1998) Pharmacol. Ther. , vol.80 , pp. 231-264
    • Wess, J.1
  • 101
    • 0037117562 scopus 로고    scopus 로고
    • Comparison of the dynamics of substrate access channels in three cytochrome P450s reveals different opening mechanisms and a novel functional role for a buried arginine
    • Winn, P.J., Ludemann, S.K., Gauges, R., Lounnas, V., and Wade, R.C. 2002. Comparison of the dynamics of substrate access channels in three cytochrome P450s reveals different opening mechanisms and a novel functional role for a buried arginine. Proc. Natl. Acad. Sci. 99: 5361-5366.
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 5361-5366
    • Winn, P.J.1    Ludemann, S.K.2    Gauges, R.3    Lounnas, V.4    Wade, R.C.5
  • 102
    • 0037762755 scopus 로고    scopus 로고
    • G Protein selectivity is regulated by multiple intracellular regions of GPCRs
    • Wong, S.K. 2002. G Protein selectivity is regulated by multiple intracellular regions of GPCRs. Neurosignals 12: 1-12.
    • (2002) Neurosignals , vol.12 , pp. 1-12
    • Wong, S.K.1
  • 103
    • 0034649373 scopus 로고    scopus 로고
    • The conserved cysteine 7.38 residue is differentially accessible in the binding-site crevices of the μ, δ, and κ opioid receptors
    • Xu, W., Chen, C., Huang, P., Li, J., de Riel, J.K., Javitch, J.A., and Liu-Chen, L. 2000. The conserved cysteine 7.38 residue is differentially accessible in the binding-site crevices of the μ, δ, and κ opioid receptors. Biochemistry 39: 13904-13915.
    • (2000) Biochemistry , vol.39 , pp. 13904-13915
    • Xu, W.1    Chen, C.2    Huang, P.3    Li, J.4    De Riel, J.K.5    Javitch, J.A.6    Liu-Chen, L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.