메뉴 건너뛰기




Volumn 58, Issue 3, 2005, Pages 644-660

Prediction of interfaces for oligomerizations of G-protein coupled receptors

Author keywords

Binomial distribution; Class A G protein coupled receptors; Conserved residue; Domain contact oligomerization; Principal component analysis

Indexed keywords

AMINO ACID; BETA 2 ADRENERGIC RECEPTOR; DOPAMINE 2 RECEPTOR; G PROTEIN COUPLED RECEPTOR; OLIGOMER; RHODOPSIN;

EID: 12944263647     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20332     Document Type: Article
Times cited : (37)

References (96)
  • 1
    • 0037082324 scopus 로고    scopus 로고
    • Target validation of G-protein coupled receptors
    • Wise A, Gearing K, Rees S. Target validation of G-protein coupled receptors. Drug Discov Today 2002;7:235-246.
    • (2002) Drug Discov Today , vol.7 , pp. 235-246
    • Wise, A.1    Gearing, K.2    Rees, S.3
  • 2
    • 0037024360 scopus 로고    scopus 로고
    • Identification of G protein-coupled receptor genes from the human genome sequence
    • Takeda S, Kadowaki S, Haga T, Takaesu H, Mitaku S. Identification of G protein-coupled receptor genes from the human genome sequence. FEBS Lett 2002;520:97-101.
    • (2002) FEBS Lett , vol.520 , pp. 97-101
    • Takeda, S.1    Kadowaki, S.2    Haga, T.3    Takaesu, H.4    Mitaku, S.5
  • 4
    • 0035318509 scopus 로고    scopus 로고
    • Oligomerization of G-protein-coupled transmitter receptors
    • Bouvier M. Oligomerization of G-protein-coupled transmitter receptors. Nat Rev Neurosci 2001;2:274-286.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 274-286
    • Bouvier, M.1
  • 5
    • 0034937698 scopus 로고    scopus 로고
    • G protein coupled receptor dimerization: Implications in modulating receptor function
    • Gomes I, Jordan BA, Gupta A, Rios C, Trapaidze N, Devi LA. G protein coupled receptor dimerization: implications in modulating receptor function. J Mol Med 2001;79:226-242.
    • (2001) J Mol Med , vol.79 , pp. 226-242
    • Gomes, I.1    Jordan, B.A.2    Gupta, A.3    Rios, C.4    Trapaidze, N.5    Devi, L.A.6
  • 6
    • 0035726693 scopus 로고    scopus 로고
    • G-protein-coupled receptor dimerization: Modulation of receptor function
    • Rios CD, Jordan BA, Gomes I, Devi LA. G-protein-coupled receptor dimerization: modulation of receptor function. Pharmacol Ther 2001;92:71-87.
    • (2001) Pharmacol Ther , vol.92 , pp. 71-87
    • Rios, C.D.1    Jordan, B.A.2    Gomes, I.3    Devi, L.A.4
  • 7
    • 0036174608 scopus 로고    scopus 로고
    • Dimerization:an emerging concept for G protein-coupled receptor ontogeny and function
    • Angers S, Salahpour A, Bouvier M. Dimerization:an emerging concept for G protein-coupled receptor ontogeny and function. Annu Rev Pharmacol Toxicol 2002;42:409-435.
    • (2002) Annu Rev Pharmacol Toxicol , vol.42 , pp. 409-435
    • Angers, S.1    Salahpour, A.2    Bouvier, M.3
  • 8
    • 0042467972 scopus 로고    scopus 로고
    • Molecular mechanisms and therapeutical implications of intramembrane receptor/receptor interactions among heptahelical receptors with examples from the striatopallidal GABA neurons
    • Agnati LF, Ferre S, Lluis C, Franco R, Fuxe K. Molecular mechanisms and therapeutical implications of intramembrane receptor/receptor interactions among heptahelical receptors with examples from the striatopallidal GABA neurons. Pharmacol Rev 2003;55:509-550.
    • (2003) Pharmacol Rev , vol.55 , pp. 509-550
    • Agnati, L.F.1    Ferre, S.2    Lluis, C.3    Franco, R.4    Fuxe, K.5
  • 9
    • 0347320632 scopus 로고    scopus 로고
    • G-protein coupled receptor oligomerization in neuroendocrine pathways
    • Kroeger KM, Pfleger KD, Eidne KA. G-protein coupled receptor oligomerization in neuroendocrine pathways. Front Neuroendocrinol 2003;24:254-278.
    • (2003) Front Neuroendocrinol , vol.24 , pp. 254-278
    • Kroeger, K.M.1    Pfleger, K.D.2    Eidne, K.A.3
  • 10
    • 1242276192 scopus 로고    scopus 로고
    • Roles of G-protein-coupled receptor dimerization
    • Terrillon S, Bouvier M. Roles of G-protein-coupled receptor dimerization. EMBO Rep 2004;5:30-34.
    • (2004) EMBO Rep , vol.5 , pp. 30-34
    • Terrillon, S.1    Bouvier, M.2
  • 12
    • 0017190266 scopus 로고
    • Negative cooperativity among beta-adrenergic receptors in frog erythrocyte membranes
    • Limbird LE, Lefkowitz RJ. Negative cooperativity among beta-adrenergic receptors in frog erythrocyte membranes. J Biol Chem 1976;251:5007-5014.
    • (1976) J Biol Chem , vol.251 , pp. 5007-5014
    • Limbird, L.E.1    Lefkowitz, R.J.2
  • 13
    • 0029753014 scopus 로고    scopus 로고
    • Agonist stimulation increases the turnover rate of beta 2AR-bound palmitate and promotes receptor depalmitoylation
    • Loisel TP, Adam L, Hebert TE, Bouvier M. Agonist stimulation increases the turnover rate of beta 2AR-bound palmitate and promotes receptor depalmitoylation. Biochemistry 1996;35:15923-15932
    • (1996) Biochemistry , vol.35 , pp. 15923-15932
    • Loisel, T.P.1    Adam, L.2    Hebert, T.E.3    Bouvier, M.4
  • 14
    • 0029666267 scopus 로고    scopus 로고
    • A peptide derived from a beta2-adrenergic receptor transmembrane domain inhibits both receptor dimerization and activation
    • Hebert TE, Moffett S, Morello JP, Loisel TP, Bichet DG, Barret C, Bouvier M. A peptide derived from a beta2-adrenergic receptor transmembrane domain inhibits both receptor dimerization and activation. J Biol Chem 1996;271:16384-16392.
    • (1996) J Biol Chem , vol.271 , pp. 16384-16392
    • Hebert, T.E.1    Moffett, S.2    Morello, J.P.3    Loisel, T.P.4    Bichet, D.G.5    Barret, C.6    Bouvier, M.7
  • 15
    • 0032519493 scopus 로고    scopus 로고
    • Functional rescue of a constitutively desensitized beta2AR through receptor dimerization
    • Hebert TE, Loisel TP, Adam L, Ethier N, Onge SS, Bouvier M. Functional rescue of a constitutively desensitized beta2AR through receptor dimerization. Biochem J 1998;330:287-293.
    • (1998) Biochem J , vol.330 , pp. 287-293
    • Hebert, T.E.1    Loisel, T.P.2    Adam, L.3    Ethier, N.4    Onge, S.S.5    Bouvier, M.6
  • 16
    • 0034724192 scopus 로고    scopus 로고
    • Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET)
    • Angers S, Salahpour A, Joly E, Hilairet S, Chelsky D, Dennis M, Bouvier M. Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET). Proc Natl Acad Sci USA 2000;97:3684-3689.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3684-3689
    • Angers, S.1    Salahpour, A.2    Joly, E.3    Hilairet, S.4    Chelsky, D.5    Dennis, M.6    Bouvier, M.7
  • 18
    • 0035958023 scopus 로고    scopus 로고
    • Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer. The human delta-opioid receptor displays constitutive oligomerization at the cell surface, which is not regulated by receptor occupancy
    • McVey M, Ramsay D, Kellett E, Rees S, Wilson S, Pope AJ, Milligan G. Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer. The human delta-opioid receptor displays constitutive oligomerization at the cell surface, which is not regulated by receptor occupancy. J Biol Chem 2001;276:14092-14099.
    • (2001) J Biol Chem , vol.276 , pp. 14092-14099
    • McVey, M.1    Ramsay, D.2    Kellett, E.3    Rees, S.4    Wilson, S.5    Pope, A.J.6    Milligan, G.7
  • 20
    • 0036462451 scopus 로고    scopus 로고
    • Oligomerization of opioid receptors:generation of novel signaling units
    • Levac BA, O'Dowd BF, George SR. Oligomerization of opioid receptors:generation of novel signaling units. Curr Opin Pharmacol 2002;2:76-81.
    • (2002) Curr Opin Pharmacol , vol.2 , pp. 76-81
    • Levac, B.A.1    O'Dowd, B.F.2    George, S.R.3
  • 21
    • 0034618268 scopus 로고    scopus 로고
    • AT1-receptor heterodimers show enhanced G-protein activation and altered receptor sequestration
    • AbdAlla S, Lother H, Quitterer U. AT1-receptor heterodimers show enhanced G-protein activation and altered receptor sequestration. Nature 2000;407:94-98.
    • (2000) Nature , vol.407 , pp. 94-98
    • AbdAlla, S.1    Lother, H.2    Quitterer, U.3
  • 22
    • 0034785580 scopus 로고    scopus 로고
    • Increased AT(1) receptor heterodimers in preeclampsia mediate enhanced angiotensin II responsiveness
    • AbdAlla S, Lother H, el Massiery A, Quitterer U. Increased AT(1) receptor heterodimers in preeclampsia mediate enhanced angiotensin II responsiveness. Nat Med 2001;7:1003-1009.
    • (2001) Nat Med , vol.7 , pp. 1003-1009
    • AbdAlla, S.1    Lother, H.2    El Massiery, A.3    Quitterer, U.4
  • 23
    • 1242274647 scopus 로고    scopus 로고
    • Heterodimerization of V1a and V2 vasopressin receptors determines the interaction with beta-arrestin and their trafficking patterns
    • Terrillon S, Barberis C, Bouvier M. Heterodimerization of V1a and V2 vasopressin receptors determines the interaction with beta-arrestin and their trafficking patterns. Proc Natl Acad Sci USA 2004;101:1548-1553.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 1548-1553
    • Terrillon, S.1    Barberis, C.2    Bouvier, M.3
  • 24
    • 10644269916 scopus 로고    scopus 로고
    • Oligomeric assembly of dopamine D(1) and glutamate NMDA receptors: Molecular mechanisms and functional implications
    • Fiorentini C, Missale C. Oligomeric assembly of dopamine D(1) and glutamate NMDA receptors: molecular mechanisms and functional implications. Biochem Soc Trans 2004;32:1025-1028.
    • (2004) Biochem Soc Trans , vol.32 , pp. 1025-1028
    • Fiorentini, C.1    Missale, C.2
  • 26
    • 0038159530 scopus 로고    scopus 로고
    • Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes
    • Liang Y, Fotiadis D, Filipek S, Saperstein DA, Palczewski K, Engel A. Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes. J Biol Chem 2003;278:21655-21662.
    • (2003) J Biol Chem , vol.278 , pp. 21655-21662
    • Liang, Y.1    Fotiadis, D.2    Filipek, S.3    Saperstein, D.A.4    Palczewski, K.5    Engel, A.6
  • 29
    • 0034688225 scopus 로고    scopus 로고
    • Direct protein-protein coupling enables cross-talk between dopamine D5 and gamma-aminobutyric acid A receptors
    • Liu F, Wan Q, Pristupa ZB, Yu XM, Wang YT, Niznik HB. Direct protein-protein coupling enables cross-talk between dopamine D5 and gamma-aminobutyric acid A receptors. Nature 2000;403:274-280.
    • (2000) Nature , vol.403 , pp. 274-280
    • Liu, F.1    Wan, Q.2    Pristupa, Z.B.3    Yu, X.M.4    Wang, Y.T.5    Niznik, H.B.6
  • 30
    • 0033516576 scopus 로고    scopus 로고
    • Identification and molecular characterization of m3 muscarinic receptor dimers
    • Zeng FY, Wess J. Identification and molecular characterization of m3 muscarinic receptor dimers. J Biol Chem 1999;274:19487-19497.
    • (1999) J Biol Chem , vol.274 , pp. 19487-19497
    • Zeng, F.Y.1    Wess, J.2
  • 31
    • 0033801789 scopus 로고    scopus 로고
    • Molecular aspects of muscarinic receptor dimerization
    • Zeng F, Wess J. Molecular aspects of muscarinic receptor dimerization. Neuropsychopharmacology 2000;23:S19-31.
    • (2000) Neuropsychopharmacology , vol.23
    • Zeng, F.1    Wess, J.2
  • 34
    • 0027533276 scopus 로고
    • Reconstitution of functional muscarinic receptors by coexpression of amino- and carboxyl-terminal receptor fragments
    • Maggio R, Vogel Z, Wess, J. Reconstitution of functional muscarinic receptors by coexpression of amino- and carboxyl-terminal receptor fragments. FEBS Lett 1993;319:195-200.
    • (1993) FEBS Lett , vol.319 , pp. 195-200
    • Maggio, R.1    Vogel, Z.2    Wess, J.3
  • 35
    • 0027467848 scopus 로고
    • Coexpression studies with mutant muscarinic/adrenergic receptors provide evidence for intermolecular "cross-talk" between G-protein-linked receptors
    • Maggio R, Vogel Z, Wess J. Coexpression studies with mutant muscarinic/adrenergic receptors provide evidence for intermolecular "cross-talk" between G-protein-linked receptors. Proc Natl Acad Sci U S A 1993;90:3103-3107.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 3103-3107
    • Maggio, R.1    Vogel, Z.2    Wess, J.3
  • 36
    • 3042551375 scopus 로고    scopus 로고
    • Ligand-induced rearrangement of the dimeric metabotropic glutamate receptor lalpha
    • Tateyama M, Abe H, Nakata H, Saito O, Kubo Y. Ligand-induced rearrangement of the dimeric metabotropic glutamate receptor lalpha. Nat Struct Mol Biol 2004;11:637-642.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 637-642
    • Tateyama, M.1    Abe, H.2    Nakata, H.3    Saito, O.4    Kubo, Y.5
  • 39
    • 0035895907 scopus 로고    scopus 로고
    • The extracellular calcium-sensing receptor dimerizes through multiple types of intermolecular interactions
    • Zhang Z, Sun S, Quinn SJ, Brown EM, Bai M. The extracellular calcium-sensing receptor dimerizes through multiple types of intermolecular interactions. J Biol Chem 2001;276:5316-5322.
    • (2001) J Biol Chem , vol.276 , pp. 5316-5322
    • Zhang, Z.1    Sun, S.2    Quinn, S.J.3    Brown, E.M.4    Bai, M.5
  • 42
    • 0038576278 scopus 로고    scopus 로고
    • The fourth transmembrane segment forms the interface of the dopamine D2 receptor homodimer
    • Guo W, Shi L, Javitch JA. The fourth transmembrane segment forms the interface of the dopamine D2 receptor homodimer. J Biol Chem 2003;278:4385-4388.
    • (2003) J Biol Chem , vol.278 , pp. 4385-4388
    • Guo, W.1    Shi, L.2    Javitch, J.A.3
  • 43
    • 0141431029 scopus 로고    scopus 로고
    • D2 dopamine receptor homodimerization is mediated by multiple sites of interaction, including an intermolecular interaction involving transmembrane domain 4
    • Lee SP, O'Dowd BF, Rajaram RD, Nguyen T, George SR. D2 dopamine receptor homodimerization is mediated by multiple sites of interaction, including an intermolecular interaction involving transmembrane domain 4. Biochemistry 2003;42:11023-11031.
    • (2003) Biochemistry , vol.42 , pp. 11023-11031
    • Lee, S.P.1    O'Dowd, B.F.2    Rajaram, R.D.3    Nguyen, T.4    George, S.R.5
  • 46
    • 0031565729 scopus 로고    scopus 로고
    • Analysis of protein-protein interaction sites using surface patches
    • Jones S, Thornton JM. Analysis of protein-protein interaction sites using surface patches. J Mol Biol 1997;272:121-132.
    • (1997) J Mol Biol , vol.272 , pp. 121-132
    • Jones, S.1    Thornton, J.M.2
  • 47
    • 0031565725 scopus 로고    scopus 로고
    • Prediction of protein-protein interaction sites using patch analysis
    • Jones S, Thornton JM. Prediction of protein-protein interaction sites using patch analysis. J Mol Biol 1997;272:133-143.
    • (1997) J Mol Biol , vol.272 , pp. 133-143
    • Jones, S.1    Thornton, J.M.2
  • 48
    • 0029913807 scopus 로고    scopus 로고
    • An evolutionary trace method defines binding surfaces common to protein families
    • Lichtarge O, Bourne HR, Cohen FE. An evolutionary trace method defines binding surfaces common to protein families. J Mol Biol 1996;257:342-358.
    • (1996) J Mol Biol , vol.257 , pp. 342-358
    • Lichtarge, O.1    Bourne, H.R.2    Cohen, F.E.3
  • 49
    • 0038356582 scopus 로고    scopus 로고
    • Predicted protein-protein interaction sites from local sequence information
    • Ofran Y, Rost B. Predicted protein-protein interaction sites from local sequence information. FEBS Lett 2003;544:236-239.
    • (2003) FEBS Lett , vol.544 , pp. 236-239
    • Ofran, Y.1    Rost, B.2
  • 50
    • 0346220017 scopus 로고    scopus 로고
    • Dimerization in aminergic G-protein-coupled receptors: Application of a hidden-site class model of evolution
    • Soyer OS, Dimmic MW, Neubig RR, Goldstein RA. Dimerization in aminergic G-protein-coupled receptors: application of a hidden-site class model of evolution. Biochemistry 2003;42:14522-14531
    • (2003) Biochemistry , vol.42 , pp. 14522-14531
    • Soyer, O.S.1    Dimmic, M.W.2    Neubig, R.R.3    Goldstein, R.A.4
  • 51
    • 0032711731 scopus 로고    scopus 로고
    • Analysis of heregulin symmetry by weighted evolutionary tracing
    • Landgraf R, Fischer D, Eisenberg D. Analysis of heregulin symmetry by weighted evolutionary tracing. Protein Eng 1999;12:943-951.
    • (1999) Protein Eng , vol.12 , pp. 943-951
    • Landgraf, R.1    Fischer, D.2    Eisenberg, D.3
  • 52
    • 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, Meng EC, Wensel TG, Lichtarge O. 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    Meng, E.C.4    Wensel, T.G.5    Lichtarge, O.6
  • 53
    • 0034644783 scopus 로고    scopus 로고
    • Analysis and prediction of functional sub-types from protein sequence alignments
    • Hannenhalli SS, Russell RB. Analysis and prediction of functional sub-types from protein sequence alignments. J Mol Biol 2000;303: 61-76.
    • (2000) J Mol Biol , vol.303 , pp. 61-76
    • Hannenhalli, S.S.1    Russell, R.B.2
  • 54
    • 0035061686 scopus 로고    scopus 로고
    • Maximum-likelihood approach for gene family evolution under functional divergence
    • Gu X. Maximum-likelihood approach for gene family evolution under functional divergence. Mol Biol Evol 2001;18:453-464.
    • (2001) Mol Biol Evol , vol.18 , pp. 453-464
    • Gu, X.1
  • 55
    • 0037470597 scopus 로고    scopus 로고
    • Automatic methods for predicting functionally important residues
    • del Sol Mesa A, Pazos F, Valencia A. Automatic methods for predicting functionally important residues. J Mol Biol 2003;326: 1289-1302.
    • (2003) J Mol Biol , vol.326 , pp. 1289-1302
    • Del Sol Mesa, A.1    Pazos, F.2    Valencia, A.3
  • 56
    • 1242339659 scopus 로고    scopus 로고
    • A family of evolution-entropy hybrid methods for ranking protein residues by importance
    • Mihalek I, Res I, Lichtarge O. A family of evolution-entropy hybrid methods for ranking protein residues by importance. J Mol Biol 2004;336:1265-1282.
    • (2004) J Mol Biol , vol.336 , pp. 1265-1282
    • Mihalek, I.1    Res, I.2    Lichtarge, O.3
  • 57
    • 0036300444 scopus 로고    scopus 로고
    • Structural clusters of evolutionary trace residues are statistically significant and common in proteins
    • Madabushi S, Yao H, Marsh M, Kristensen DM, Philippi A, Sowa ME, Lichtarge O. Structural clusters of evolutionary trace residues are statistically significant and common in proteins. J Mol Biol 2002;316:139-154.
    • (2002) J Mol Biol , vol.316 , pp. 139-154
    • Madabushi, S.1    Yao, H.2    Marsh, M.3    Kristensen, D.M.4    Philippi, A.5    Sowa, M.E.6    Lichtarge, O.7
  • 59
    • 0034677745 scopus 로고    scopus 로고
    • Subtypes of the somatostatin receptor assemble as functional homo- and heterodimers
    • Rocheville M, Lange DC, Kumar U, Sasi R, Patel RC, Patel YC. Subtypes of the somatostatin receptor assemble as functional homo- and heterodimers. J Biol Chem 2000;275:7862-7869.
    • (2000) J Biol Chem , vol.275 , pp. 7862-7869
    • Rocheville, M.1    Lange, D.C.2    Kumar, U.3    Sasi, R.4    Patel, R.C.5    Patel, Y.C.6
  • 60
    • 0033578005 scopus 로고    scopus 로고
    • G-protein-coupled receptor heterodimerization modulates receptor function
    • Jordan BA, Devi LA. G-protein-coupled receptor heterodimerization modulates receptor function. Nature 1999;399:697-700.
    • (1999) Nature , vol.399 , pp. 697-700
    • Jordan, B.A.1    Devi, L.A.2
  • 61
    • 0034714335 scopus 로고    scopus 로고
    • Oligomerization of mu- and delta-opioid receptors. Generation of novel functional properties
    • George SR, Fan T, Xie Z, Tse R, Tam V, Varghese G, O'Dowd BF. Oligomerization of mu- and delta-opioid receptors. Generation of novel functional properties. J Biol Chem 2000;275:26128-26135.
    • (2000) J Biol Chem , vol.275 , pp. 26128-26135
    • George, S.R.1    Fan, T.2    Xie, Z.3    Tse, R.4    Tam, V.5    Varghese, G.6    O'Dowd, B.F.7
  • 63
    • 0035793079 scopus 로고    scopus 로고
    • Oligomerization of opioid receptors with beta 2-adrenergic receptors: A role in trafficking and mitogen-activated protein kinase activation
    • Jordan BA, Trapaidze N, Gomes I, Nivarthi R, Devi LA. Oligomerization of opioid receptors with beta 2-adrenergic receptors: a role in trafficking and mitogen-activated protein kinase activation. Proc Natl Acad Sci USA 2001;98:343-348.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 343-348
    • Jordan, B.A.1    Trapaidze, N.2    Gomes, I.3    Nivarthi, R.4    Devi, L.A.5
  • 65
    • 0032515074 scopus 로고    scopus 로고
    • A transmembrane domain-derived peptide inhibits D1 dopamine receptor function without affecting receptor oligomerization
    • George SR, Lee SP, Varghese G, Zeman PR, Seeman P, Ng GY, O'Dowd BF. A transmembrane domain-derived peptide inhibits D1 dopamine receptor function without affecting receptor oligomerization. J Biol Chem 1998;273:30244-30248.
    • (1998) J Biol Chem , vol.273 , pp. 30244-30248
    • George, S.R.1    Lee, S.P.2    Varghese, G.3    Zeman, P.R.4    Seeman, P.5    Ng, G.Y.6    O'Dowd, B.F.7
  • 68
    • 0037648337 scopus 로고    scopus 로고
    • Structure-based analysis of GPCR function: Conformational adaptation of both agonist and receptor upon leukotriene B4 binding to recombinant BLT1
    • Baneres JL, Martin A, Hullot P, Girard JP, Rossi JC, Parello J. Structure-based analysis of GPCR function: conformational adaptation of both agonist and receptor upon leukotriene B4 binding to recombinant BLT1. J Mol Biol 2003;329:801-814.
    • (2003) J Mol Biol , vol.329 , pp. 801-814
    • Baneres, J.L.1    Martin, A.2    Hullot, P.3    Girard, J.P.4    Rossi, J.C.5    Parello, J.6
  • 69
    • 0038392702 scopus 로고    scopus 로고
    • Structure-based analysis of GPCR function: Evidence for a novel pentameric assembly between the dimeric leukotriene B4 receptor BLT1 and the G-protein
    • Baneres JL, Parello J. Structure-based analysis of GPCR function: evidence for a novel pentameric assembly between the dimeric leukotriene B4 receptor BLT1 and the G-protein. J Mol Biol 2003;329:815-829.
    • (2003) J Mol Biol , vol.329 , pp. 815-829
    • Baneres, J.L.1    Parello, J.2
  • 70
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG. The CLUSTAL X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 1997;25:4876-4882.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 71
    • 12944332482 scopus 로고    scopus 로고
    • http://www.mbio.ncsu.edu/BioEdit/bioedit.html
  • 72
    • 0036139211 scopus 로고    scopus 로고
    • MEGA2: Molecular evolutionary genetics analysis software
    • Kumar S, Tamura K, Jakobsen IB, Nei M. MEGA2: molecular evolutionary genetics analysis software. Bioinformatics 2001;17: 1244-1245.
    • (2001) Bioinformatics , vol.17 , pp. 1244-1245
    • Kumar, S.1    Tamura, K.2    Jakobsen, I.B.3    Nei, M.4
  • 73
    • 0035178383 scopus 로고    scopus 로고
    • Protein-protein interfaces: Analysis of amino acid conservation in homodimers
    • Valdar WS, Thornton JM. Protein-protein interfaces: analysis of amino acid conservation in homodimers. Proteins 2001;42:108-124.
    • (2001) Proteins , vol.42 , pp. 108-124
    • Valdar, W.S.1    Thornton, J.M.2
  • 74
    • 0028153788 scopus 로고
    • A mutation data matrix for transmembrane proteins
    • Jones DT, Taylor WR, Thornton JM. A mutation data matrix for transmembrane proteins. FEBS Lett 1994;339:269-275.
    • (1994) FEBS Lett , vol.339 , pp. 269-275
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 75
    • 0028043552 scopus 로고
    • Position-based sequence weights
    • Henikoff S, Henikoff JG. Position-based sequence weights. J Mol Biol 1994;243:574-578.
    • (1994) J Mol Biol , vol.243 , pp. 574-578
    • Henikoff, S.1    Henikoff, J.G.2
  • 76
    • 12944255037 scopus 로고    scopus 로고
    • http://wolf.bms.umist.ac.uk/naccess/naccess.html
  • 77
    • 12944274039 scopus 로고    scopus 로고
    • http://www.umass.edu/microbio/rasmol/
  • 78
    • 12944277642 scopus 로고    scopus 로고
    • http://kr.expasy.org/spdbv/
  • 79
    • 0031547966 scopus 로고    scopus 로고
    • Electrostatic complementarity at protein/protein interfaces
    • McCoy AJ, Chandana Epa V, Colman PM. Electrostatic complementarity at protein/protein interfaces. J Mol Biol 1997;268:570-584.
    • (1997) J Mol Biol , vol.268 , pp. 570-584
    • McCoy, A.J.1    Chandana Epa, V.2    Colman, P.M.3
  • 80
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan AA, Thorn KS. Anatomy of hot spots in protein interfaces. J Mol Biol 1998;280:1-9.
    • (1998) J Mol Biol , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 81
    • 0037093645 scopus 로고    scopus 로고
    • Dissecting protein-protein recognition sites
    • Chakrabarti P, Janin J. Dissecting protein-protein recognition sites. Proteins 2002;47:334-343.
    • (2002) Proteins , vol.47 , pp. 334-343
    • Chakrabarti, P.1    Janin, J.2
  • 82
    • 0037609791 scopus 로고    scopus 로고
    • Protein-protein interactions: Structurally conserved residues distinguish between binding sites and exposed protein surfaces
    • Ma B, Elkayam T, Wolfson H, Nussinov R. Protein-protein interactions: structurally conserved residues distinguish between binding sites and exposed protein surfaces. Proc Natl Acad Sci USA 2003;100:5772-5777.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5772-5777
    • Ma, B.1    Elkayam, T.2    Wolfson, H.3    Nussinov, R.4
  • 83
    • 0037229456 scopus 로고    scopus 로고
    • Analysing six types of protein-protein interfaces
    • Ofran Y, Rost B. Analysing six types of protein-protein interfaces. J Mol Biol 2003;325:377-387.
    • (2003) J Mol Biol , vol.325 , pp. 377-387
    • Ofran, Y.1    Rost, B.2
  • 84
    • 0037474541 scopus 로고    scopus 로고
    • Structural characterisation and functional significance of transient protein-protein interactions
    • Nooren IM, Thornton JM. Structural characterisation and functional significance of transient protein-protein interactions. J Mol Biol 2003;325:991-1018.
    • (2003) J Mol Biol , vol.325 , pp. 991-1018
    • Nooren, I.M.1    Thornton, J.M.2
  • 85
    • 0346733329 scopus 로고    scopus 로고
    • Are protein-protein interfaces more conserved in sequence than the rest of the protein surface?
    • Caffrey DR, Somaroo S, Hughes JD, Mintseris J, Huang ES. Are protein-protein interfaces more conserved in sequence than the rest of the protein surface? Protein Sci 2004;13:190-202.
    • (2004) Protein Sci , vol.13 , pp. 190-202
    • Caffrey, D.R.1    Somaroo, S.2    Hughes, J.D.3    Mintseris, J.4    Huang, E.S.5
  • 86
    • 0034213559 scopus 로고    scopus 로고
    • Conservation of polar residues as hot spots at protein interfaces
    • Hu Z, Ma B, Wolfson H, Nussinov R. Conservation of polar residues as hot spots at protein interfaces. Proteins 2000;39:331-342.
    • (2000) Proteins , vol.39 , pp. 331-342
    • Hu, Z.1    Ma, B.2    Wolfson, H.3    Nussinov, R.4
  • 90
    • 0030861647 scopus 로고    scopus 로고
    • Adenosine-dopamine receptor-receptor interactions as an integrative mechanism in the basal ganglia
    • Ferre S, Fredholm BB, Morelli M, Popoli P, Fuxe K. Adenosine-dopamine receptor-receptor interactions as an integrative mechanism in the basal ganglia. Trends Neurosci 1997;20:482-487.
    • (1997) Trends Neurosci , vol.20 , pp. 482-487
    • Ferre, S.1    Fredholm, B.B.2    Morelli, M.3    Popoli, P.4    Fuxe, K.5
  • 93
    • 0035979146 scopus 로고    scopus 로고
    • The Calpha -H...O hydrogen bond: A determinant of stability and specificity in transmembrane helix interactions
    • Senes A, Ubarretxena-Belandia I, Engelman DM. The Calpha -H...O hydrogen bond: a determinant of stability and specificity in transmembrane helix interactions. Proc Natl Acad Sci USA 2001;98:9056-9061.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 9056-9061
    • Senes, A.1    Ubarretxena-Belandia, I.2    Engelman, D.M.3
  • 94
    • 0024110575 scopus 로고
    • Cysteine residues 110 and 187 are essential for the formation of correct structure in bovine rhodopsin
    • Karnik SS, Sakmar TP, Chen HB, Khorana HG. Cysteine residues 110 and 187 are essential for the formation of correct structure in bovine rhodopsin. Proc Natl Acad Sci USA 1988;85:8459-8463.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 8459-8463
    • Karnik, S.S.1    Sakmar, T.P.2    Chen, H.B.3    Khorana, H.G.4
  • 96
    • 0026609104 scopus 로고
    • The distribution of charged amino acids in mitochondrial inner-membrane proteins suggests different modes of membrane integration for nuclearly and mitochondrially encoded proteins
    • Gavel Y, von Heijne G. The distribution of charged amino acids in mitochondrial inner-membrane proteins suggests different modes of membrane integration for nuclearly and mitochondrially encoded proteins. Eur J Biochem 1992;205:1207-1215.
    • (1992) Eur J Biochem , vol.205 , pp. 1207-1215
    • Gavel, Y.1    Von Heijne, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.