메뉴 건너뛰기




Volumn 47, Issue 36, 2008, Pages 9574-9581

Use of multidimensional fluorescence resonance energy transfer to establish the orientation of cholecystokinin docked at the type A cholecystokinin receptor

Author keywords

[No Author keywords available]

Indexed keywords

ENERGY TRANSFER; LUMINESCENCE; RESONANCE; THREE DIMENSIONAL;

EID: 51549112505     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800734w     Document Type: Article
Times cited : (9)

References (30)
  • 5
    • 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
  • 6
    • 0027933763 scopus 로고
    • Locating ligand-binding sites in 7TM receptors by protein engineering
    • Schwartz, T. W. (1994) Locating ligand-binding sites in 7TM receptors by protein engineering. Curr. Opin. Biotechnol. 5, 434-444.
    • (1994) Curr. Opin. Biotechnol , vol.5 , pp. 434-444
    • Schwartz, T.W.1
  • 7
    • 33644841711 scopus 로고    scopus 로고
    • Cholecystokinin and gastrin receptors
    • Dufresne, M., Seva, C., and Fourmy, D. (2006) Cholecystokinin and gastrin receptors. Physiol. Rev. 86, 805-847.
    • (2006) Physiol. Rev , vol.86 , pp. 805-847
    • Dufresne, M.1    Seva, C.2    Fourmy, D.3
  • 8
    • 0030969362 scopus 로고    scopus 로고
    • Cholecystokinin cells
    • Liddle, R. A. (1997) Cholecystokinin cells. Annu. Rev. Physiol. 59, 221-242.
    • (1997) Annu. Rev. Physiol , vol.59 , pp. 221-242
    • Liddle, R.A.1
  • 9
    • 46149118170 scopus 로고    scopus 로고
    • Structural basis of cholecystokinin receptor binding and regulation
    • Miller, L. J., and Gao, F. (2008) Structural basis of cholecystokinin receptor binding and regulation. Pharmacol. Ther. 119, 83-95.
    • (2008) Pharmacol. Ther , vol.119 , pp. 83-95
    • Miller, L.J.1    Gao, F.2
  • 10
    • 0036233457 scopus 로고    scopus 로고
    • Refinement of the conformation of a critical region of charge-charge interaction between cholecystokinin and its receptor
    • Ding, X. Q., Pinon, D. I., Furse, K. E., Lybrand, T. P., and Miller, L. J. (2002) Refinement of the conformation of a critical region of charge-charge interaction between cholecystokinin and its receptor. Mol. Pharmacol. 61, 1041-1052.
    • (2002) Mol. Pharmacol , vol.61 , pp. 1041-1052
    • Ding, X.Q.1    Pinon, D.I.2    Furse, K.E.3    Lybrand, T.P.4    Miller, L.J.5
  • 11
    • 33645783040 scopus 로고    scopus 로고
    • Probing a model of a GPCR/ligand complex in an explicit membrane environment: The human cholecystokinin-1 receptor
    • Henin, J., Maigret, B., Tarek, M., Escrieut, C., Fourmy, D., and Chipot, C. (2006) Probing a model of a GPCR/ligand complex in an explicit membrane environment: the human cholecystokinin-1 receptor. Biophys. J. 90, 1232-1240.
    • (2006) Biophys. J , vol.90 , pp. 1232-1240
    • Henin, J.1    Maigret, B.2    Tarek, M.3    Escrieut, C.4    Fourmy, D.5    Chipot, C.6
  • 12
    • 0032557448 scopus 로고    scopus 로고
    • Direct identification of a second distinct site of contact between cholecystokinin and its receptor
    • Hadac, E. M., Pinon, D. I., Ji, Z., Holicky, E. L., Henne, R. M., Lybrand, T. P., and Miller, L. J. (1998) Direct identification of a second distinct site of contact between cholecystokinin and its receptor. J. Biol. Chem. 273, 12988-12993.
    • (1998) J. Biol. Chem , vol.273 , pp. 12988-12993
    • Hadac, E.M.1    Pinon, D.I.2    Ji, Z.3    Holicky, E.L.4    Henne, R.M.5    Lybrand, T.P.6    Miller, L.J.7
  • 13
    • 0030846864 scopus 로고    scopus 로고
    • Direct identification of a distinct site of interaction between the carboxyl-terminal residue of cholecystokinin and the type A cholecystokinin receptor using photoaffinity labeling
    • Ji, Z., Hadac, E. M., Henne, R. M., Patel, S. A., Lybrand, T. P., and Miller, L. J. (1997) Direct identification of a distinct site of interaction between the carboxyl-terminal residue of cholecystokinin and the type A cholecystokinin receptor using photoaffinity labeling. J. Biol. Chem. 272, 24393-24401.
    • (1997) J. Biol. Chem , vol.272 , pp. 24393-24401
    • Ji, Z.1    Hadac, E.M.2    Henne, R.M.3    Patel, S.A.4    Lybrand, T.P.5    Miller, L.J.6
  • 14
    • 0035830920 scopus 로고    scopus 로고
    • Refinement of the structure of the ligand-occupied cholecystokinin receptor using a photolabile amino-terminal probe
    • Ding, X. Q., Dolu, V., Hadac, E. M., Holicky, E. L., Pinon, D. I., Lybrand, T. P., and Miller, L. J. (2001) Refinement of the structure of the ligand-occupied cholecystokinin receptor using a photolabile amino-terminal probe. J. Biol. Chem. 276, 4236-4244.
    • (2001) J. Biol. Chem , vol.276 , pp. 4236-4244
    • Ding, X.Q.1    Dolu, V.2    Hadac, E.M.3    Holicky, E.L.4    Pinon, D.I.5    Lybrand, T.P.6    Miller, L.J.7
  • 16
    • 15644364730 scopus 로고    scopus 로고
    • Identification of two amino acids of the human cholecystokinin-A receptor that interact with the N-terminal moiety of cholecystokinin
    • Kennedy, K., Gigoux, V., Escrieut, C., Maigret, B., Martinez, J., Moroder, L., Frehel, D., Gully, D., Vaysse, N., and Fourmy, D. (1997) Identification of two amino acids of the human cholecystokinin-A receptor that interact with the N-terminal moiety of cholecystokinin. J. Biol. Chem. 272, 2920-2926.
    • (1997) J. Biol. Chem , vol.272 , pp. 2920-2926
    • Kennedy, K.1    Gigoux, V.2    Escrieut, C.3    Maigret, B.4    Martinez, J.5    Moroder, L.6    Frehel, D.7    Gully, D.8    Vaysse, N.9    Fourmy, D.10
  • 17
    • 18544378433 scopus 로고    scopus 로고
    • The biologically crucial C terminus of cholecystokinin and the non-peptide agonist SR-146,131 share a common binding site in the human CCK1 receptor. Evidence for a crucial role of Met-121 in the activation process
    • Escrieut, C., Gigoux, V., Archer, E., Verrier, S., Maigret, B., Behrendt, R., Moroder, L., Bignon, E., Silvente-Poirot, S., Pradayrol, L., and Fourmy, D. (2002) The biologically crucial C terminus of cholecystokinin and the non-peptide agonist SR-146,131 share a common binding site in the human CCK1 receptor. Evidence for a crucial role of Met-121 in the activation process. J. Biol. Chem. 277, 7546-7555.
    • (2002) J. Biol. Chem , vol.277 , pp. 7546-7555
    • Escrieut, C.1    Gigoux, V.2    Archer, E.3    Verrier, S.4    Maigret, B.5    Behrendt, R.6    Moroder, L.7    Bignon, E.8    Silvente-Poirot, S.9    Pradayrol, L.10    Fourmy, D.11
  • 18
    • 0033575274 scopus 로고    scopus 로고
    • Arginine 336 and asparagine 333 of the human cholecystokinin-A receptor binding site interact with the penultimate aspartic acid and the C-terminal amide of cholecystokinin
    • Gigoux, V., Escrieut, C., Fehrentz, J. A., Poirot, S., Maigret, B., Moroder, L., Gully, D., Martinez, J., Vaysse, N., and Fourmy, D. (1999) Arginine 336 and asparagine 333 of the human cholecystokinin-A receptor binding site interact with the penultimate aspartic acid and the C-terminal amide of cholecystokinin. J. Biol. Chem. 274, 20457-20464.
    • (1999) J. Biol. Chem , vol.274 , pp. 20457-20464
    • Gigoux, V.1    Escrieut, C.2    Fehrentz, J.A.3    Poirot, S.4    Maigret, B.5    Moroder, L.6    Gully, D.7    Martinez, J.8    Vaysse, N.9    Fourmy, D.10
  • 20
    • 36349035022 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer analysis of secretin docking to its receptor: Mapping distances between residues distributed throughout the ligand pharmacophore and distinct receptor residues
    • Harikumar, K. G., Lam, P. C., Dong, M., Sexton, P. M., Abagyan, R., and Miller, L. J. (2007) Fluorescence resonance energy transfer analysis of secretin docking to its receptor: mapping distances between residues distributed throughout the ligand pharmacophore and distinct receptor residues. J. Biol. Chem. 282, 32834-32843.
    • (2007) J. Biol. Chem , vol.282 , pp. 32834-32843
    • Harikumar, K.G.1    Lam, P.C.2    Dong, M.3    Sexton, P.M.4    Abagyan, R.5    Miller, L.J.6
  • 21
    • 21444436216 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer analysis of the antagonist- and partial agonist-occupied states of the cholecystokinin receptor
    • Harikumar, K. G., and Miller, L. J. (2005) Fluorescence resonance energy transfer analysis of the antagonist- and partial agonist-occupied states of the cholecystokinin receptor. J. Biol. Chem. 280, 18631-18635.
    • (2005) J. Biol. Chem , vol.280 , pp. 18631-18635
    • Harikumar, K.G.1    Miller, L.J.2
  • 22
    • 1642454586 scopus 로고    scopus 로고
    • Measurement of intermolecular distances for the natural agonist Peptide docked at the cholecystokinin receptor expressed in situ using fluorescence resonance energy transfer
    • Harikumar, K. G., Pinon, D. I., Wessels, W. S., Dawson, E. S., Lybrand, T. P., Prendergast, F. G., and Miller, L. J. (2004) Measurement of intermolecular distances for the natural agonist Peptide docked at the cholecystokinin receptor expressed in situ using fluorescence resonance energy transfer. Mol. Pharmacol. 65, 28-35.
    • (2004) Mol. Pharmacol , vol.65 , pp. 28-35
    • Harikumar, K.G.1    Pinon, D.I.2    Wessels, W.S.3    Dawson, E.S.4    Lybrand, T.P.5    Prendergast, F.G.6    Miller, L.J.7
  • 23
    • 33748754344 scopus 로고    scopus 로고
    • Fluorescent indicators distributed throughout the pharmacophore of cholecystokinin provide insights into distinct modes of binding and activation of type A and B cholecystokinin receptors
    • Harikumar, K. G., Pinon, D. I., and Miller, L. J. (2006) Fluorescent indicators distributed throughout the pharmacophore of cholecystokinin provide insights into distinct modes of binding and activation of type A and B cholecystokinin receptors. J. Biol. Chem. 281, 27072-27080.
    • (2006) J. Biol. Chem , vol.281 , pp. 27072-27080
    • Harikumar, K.G.1    Pinon, D.I.2    Miller, L.J.3
  • 24
    • 0038744320 scopus 로고    scopus 로고
    • Disulfide bond structure and accessibility of cysteines in the ectodomain of the cholecystokinin receptor: Specific monoreactive receptor constructs examine charge-sensitivity of loop regions
    • Ding, X. Q., Dolu, V., Hadac, E. M., Schuetz, M., and Miller, L. J. (2003) Disulfide bond structure and accessibility of cysteines in the ectodomain of the cholecystokinin receptor: specific monoreactive receptor constructs examine charge-sensitivity of loop regions. Recep. Channels 9, 83-91.
    • (2003) Recep. Channels , vol.9 , pp. 83-91
    • Ding, X.Q.1    Dolu, V.2    Hadac, E.M.3    Schuetz, M.4    Miller, L.J.5
  • 25
    • 0037166311 scopus 로고    scopus 로고
    • Environment and mobility of a series of fluorescent reporters at the amino terminus of structurally related peptide agonists and antagonists bound to the cholecystokinin receptor
    • Harikumar, K. G., Pinon, D. I., Wessels, W. S., Prendergast, F. G., and Miller, L. J. (2002) Environment and mobility of a series of fluorescent reporters at the amino terminus of structurally related peptide agonists and antagonists bound to the cholecystokinin receptor. J. Biol. Chem. 277, 18552-18560.
    • (2002) J. Biol. Chem , vol.277 , pp. 18552-18560
    • Harikumar, K.G.1    Pinon, D.I.2    Wessels, W.S.3    Prendergast, F.G.4    Miller, L.J.5
  • 26
    • 0018267881 scopus 로고
    • Effect of the orientation of donor and acceptor on the probability of energy transfer involving electronic transitions of mixed polarization
    • Haas, E., Katchalski-Katzir, E., and Steinberg, I. Z. (1978) Effect of the orientation of donor and acceptor on the probability of energy transfer involving electronic transitions of mixed polarization. Biochemistry 17, 5064-5070.
    • (1978) Biochemistry , vol.17 , pp. 5064-5070
    • Haas, E.1    Katchalski-Katzir, E.2    Steinberg, I.Z.3
  • 28
    • 4944226721 scopus 로고    scopus 로고
    • Key differences in molecular complexes of the cholecystokinin receptor with structurally related peptide agonist, partial agonist, and antagonist
    • Arlander, S. J., Dong, M., Ding, X. Q., Pinon, D. I., and Miller, L. J. (2004) Key differences in molecular complexes of the cholecystokinin receptor with structurally related peptide agonist, partial agonist, and antagonist. Mol. Pharmacol. 66, 545-552.
    • (2004) Mol. Pharmacol , vol.66 , pp. 545-552
    • Arlander, S.J.1    Dong, M.2    Ding, X.Q.3    Pinon, D.I.4    Miller, L.J.5
  • 29
    • 0028913136 scopus 로고
    • Fluorescence resonance energy transfer
    • Selvin, P. R. (1995) Fluorescence resonance energy transfer. Methods Enzymol. 246, 300-334.
    • (1995) Methods Enzymol , vol.246 , pp. 300-334
    • Selvin, P.R.1
  • 30
    • 0025249790 scopus 로고
    • Role of extracellular disulfide-bonded cysteines in the ligand binding function of the beta 2-adrenergic receptor
    • Dohlman, H. G., Caron, M. G., DeBlasi, A., Frielle, T., and Lefkowitz, R. J. (1990) Role of extracellular disulfide-bonded cysteines in the ligand binding function of the beta 2-adrenergic receptor. Biochemistry 29, 2335-2342.
    • (1990) Biochemistry , vol.29 , pp. 2335-2342
    • Dohlman, H.G.1    Caron, M.G.2    DeBlasi, A.3    Frielle, T.4    Lefkowitz, R.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.