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Volumn 48, Issue 23, 2009, Pages 5303-5312

Elucidation of the molecular basis of cholecystokinin peptide docking to its receptor using site-specific intrinsic photoaffinity labeling and molecular modeling

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE PROBE; ADENOSINE RECEPTOR; ADRENERGIC RECEPTORS; COVALENT ATTACHMENT; DRUG DEVELOPMENT; EXPERIMENTAL DATA; EXTRACELLULAR LOOPS; FLUORESCENCE RESONANCE ENERGY TRANSFER; G PROTEIN COUPLED RECEPTORS; HOMOLOGY MODELS; LIGAND BINDING; MOLECULAR BASIS; NATURAL PEPTIDE; PEPTIDE HORMONES; PHOTOAFFINITY LABELING; PROTEOLYTIC PEPTIDES; RECEPTOR MODEL; REFINED MODEL; SITE-SPECIFIC; STRUCTURAL BASIS; STRUCTURAL DETERMINATION; WILD TYPES; WORK FOCUS;

EID: 67049100554     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9004705     Document Type: Article
Times cited : (19)

References (37)
  • 5
    • 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
  • 7
    • 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
  • 8
    • 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
  • 9
    • 21744435941 scopus 로고    scopus 로고
    • Differential spatial approximation between cholecystokinin residue 30 and receptor residues in active and inactive conformations
    • Dong, M., Hadac, E. M., Pinon, D. I., and Miller, L. J. (2005) Differential spatial approximation between cholecystokinin residue 30 and receptor residues in active and inactive conformations. Mol. Pharmacol. 67, 1892-1900.
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1892-1900
    • Dong, M.1    Hadac, E.M.2    Pinon, D.I.3    Miller, L.J.4
  • 10
    • 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
  • 11
    • 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
  • 13
    • 0023645714 scopus 로고
    • Analysis of the carbohydrate composition of the pancreatic plasma-lemmal glycoprotein affinity labeled by short probes for the cholecystokinin receptor
    • Pearson, R. K., Miller, L. J., Hadac, E. M., and Powers, S. P. (1987) Analysis of the carbohydrate composition of the pancreatic plasma-lemmal glycoprotein affinity labeled by short probes for the cholecystokinin receptor. J. Biol. Chem. 262, 13850-13856.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13850-13856
    • Pearson, R.K.1    Miller, L.J.2    Hadac, E.M.3    Powers, S.P.4
  • 14
    • 0024009303 scopus 로고
    • Use of N,O-bis-Fmoc-D-Tyr-ONSu for introduction of an oxidative iodination site into cholecystokinin family peptides
    • Powers, S. P., Pinon, D. I., and Miller, L. J. (1988) Use of N,O-bis-Fmoc-D-Tyr-ONSu for introduction of an oxidative iodination site into cholecystokinin family peptides. Int. J. Pept. Protein Res. 31, 429-434.
    • (1988) Int. J. Pept. Protein Res. , vol.31 , pp. 429-434
    • Powers, S.P.1    Pinon, D.I.2    Miller, L.J.3
  • 15
    • 0029791442 scopus 로고    scopus 로고
    • Relationship between native and recombinant cholecystokinin receptors: Role of differential glycosylation
    • Hadac, E. M., Ghanekar, D. V., Holicky, E. L., Pinon, D. I., Dougherty, R. W., and Miller, L. J. (1996) Relationship between native and recombinant cholecystokinin receptors: Role of differential glycosylation. Pancreas 13, 130-139. (Pubitemid 26266223)
    • (1996) Pancreas , vol.13 , Issue.2 , pp. 130-139
    • Hadac, E.M.1    Ghanekar, D.V.2    Holicky, E.L.3    Pinon, D.I.4    Dougherty, R.W.5    Miller, L.J.6
  • 16
    • 7344250633 scopus 로고    scopus 로고
    • Met-195 of the cholecystokinin-A receptor interacts with the sulfated tyrosine of cholecystokinin and is crucial for receptor transition to high affinity state
    • Gigoux, V., Escrieut, C., Silvente-Poirot, S., Maigret, B., Gouilleux, L., Fehrentz, J. A., Gully, D., Moroder, L., Vaysse, N., and Fourmy, D. (1998) Met-195 of the cholecystokinin-A receptor interacts with the sulfated tyrosine of cholecystokinin and is crucial for receptor transition to high affinity state. J. Biol. Chem. 273, 14380-14386.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14380-14386
    • Gigoux, V.1    Escrieut, C.2    Silvente-Poirot, S.3    Maigret, B.4    Gouilleux, L.5    Fehrentz, J.A.6    Gully, D.7    Moroder, L.8    Vaysse, N.9    Fourmy, D.10
  • 17
    • 0038744320 scopus 로고    scopus 로고
    • Disulfide bond structure and accessibility of cyteines in the ectodomain of the cholecystokinin receptor: Specific mono-reactive receptor constructs examine charge-sensitivity of loop regions
    • DOI 10.1080/10606820308249
    • 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 mono-reactive receptor constructs examine charge-sensitivity of loop regions. Receptors Channels 9, 83-91. (Pubitemid 36546716)
    • (2003) Receptors and Channels , vol.9 , Issue.2 , pp. 83-91
    • Ding, X.-Q.1    Dolu, V.2    Hadac, E.M.3    Schuetz, M.4    Miller, L.J.5
  • 18
    • 15844385219 scopus 로고    scopus 로고
    • Multiple extracellular loop domains contribute critical determinants for agonist binding and activation of the secretin receptor
    • Holtmann, M. H., Ganguli, S., Hadac, E. M., Dolu, V., and Miller, L. J. (1996) Multiple extracellular loop domains contribute critical determinants for agonist binding and activation of the secretin receptor. J. Biol. Chem. 271, 14944-14949.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14944-14949
    • Holtmann, M.H.1    Ganguli, S.2    Hadac, E.M.3    Dolu, V.4    Miller, L.J.5
  • 19
    • 0019061918 scopus 로고
    • Ligand: A versatile computerized approach for characterization of ligand-binding systems
    • Munson, P. J., and Rodbard, D. (1980) Ligand: A versatile computerized approach for characterization of ligand-binding systems. Anal. Biochem. 107, 220-239.
    • (1980) Anal. Biochem. , vol.107 , pp. 220-239
    • Munson, P.J.1    Rodbard, D.2
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0033534683 scopus 로고    scopus 로고
    • Demonstration of a direct interaction between residue 22 in the carboxyl-terminal half of secretin and the amino-terminal tail of the secretin receptor using photoaffinity labeling
    • Dong, M., Wang, Y., Pinon, D. I., Hadac, E. M., and Miller, L. J. (1999) Demonstration of a direct interaction between residue 22 in the carboxyl-terminal half of secretin and the amino-terminal tail of the secretin receptor using photoaffinity labeling. J. Biol. Chem. 274, 903-909.
    • (1999) J. Biol. Chem. , vol.274 , pp. 903-909
    • Dong, M.1    Wang, Y.2    Pinon, D.I.3    Hadac, E.M.4    Miller, L.J.5
  • 23
    • 0033516657 scopus 로고    scopus 로고
    • Identification of an interaction between residue 6 of the natural peptide ligand and a distinct residue within the amino-terminal tail of the secretin receptor
    • Dong, M., Wang, Y., Hadac, E. M., Pinon, D. I., Holicky, E., and Miller, L. J. (1999) Identification of an interaction between residue 6 of the natural peptide ligand and a distinct residue within the amino-terminal tail of the secretin receptor. J. Biol. Chem. 274, 19161-19167.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19161-19167
    • Dong, M.1    Wang, Y.2    Hadac, E.M.3    Pinon, D.I.4    Holicky, E.5    Miller, L.J.6
  • 24
    • 84986522918 scopus 로고
    • ICM: A new method for protein modeling and design: Applications to docking and structure prediction from the distorted native confirmation
    • Abagyan, R., Totrov, M., and Kuznetsov, D. (1994) ICM: A new method for protein modeling and design: Applications to docking and structure prediction from the distorted native confirmation. J. Comput. Chem. 15, 488-506.
    • (1994) J. Comput. Chem. , vol.15 , pp. 488-506
    • Abagyan, R.1    Totrov, M.2    Kuznetsov, D.3
  • 25
    • 0027955787 scopus 로고
    • Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins
    • Abagyan, R., and Totrov, M. (1994) Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins. J. Mol. Biol. 235, 983-1002.
    • (1994) J. Mol. Biol. , vol.235 , pp. 983-1002
    • Abagyan, R.1    Totrov, M.2
  • 28
    • 47949116776 scopus 로고    scopus 로고
    • Spatial approximation between secretin residue five and the third extracellular loop of its receptor provides new insight into the molecular basis of natural agonist binding
    • Dong, M., Lam, P. C., Pinon, D. I., Sexton, P. M., Abagyan, R., and Miller, L. J. (2008) Spatial approximation between secretin residue five and the third extracellular loop of its receptor provides new insight into the molecular basis of natural agonist binding. Mol. Pharmacol. 74, 413-422.
    • (2008) Mol. Pharmacol. , vol.74 , pp. 413-422
    • Dong, M.1    Lam, P.C.2    Pinon, D.I.3    Sexton, P.M.4    Abagyan, R.5    Miller, L.J.6
  • 29
    • 0033539640 scopus 로고    scopus 로고
    • Molecular complex of cholecystokinin-8 and N-terminus of the cholecystokinin a receptor by NMR spectroscopy
    • Pellegrini, M., and Mierke, D. F. (1999) Molecular complex of cholecystokinin-8 and N-terminus of the cholecystokinin A receptor by NMR spectroscopy. Biochemistry 38, 14775-14783. (Pubitemid 129517621)
    • (1999) Biochemistry , vol.38 , Issue.45 , pp. 14775-14783
    • Pellegrini, M.1    Mierke, D.F.2
  • 30
    • 51549112505 scopus 로고    scopus 로고
    • Use of multidimensional fluorescence resonance energy transfer to establish the orientation of cholecystokinin docked at the type A cholecystokinin receptor
    • Harikumar, K. G., Gao, F., Pinon, D. I., and Miller, L. J. (2008) Use of multidimensional fluorescence resonance energy transfer to establish the orientation of cholecystokinin docked at the type A cholecystokinin receptor. Biochemistry 47, 9574-9581.
    • (2008) Biochemistry , vol.47 , pp. 9574-9581
    • Harikumar, K.G.1    Gao, F.2    Pinon, D.I.3    Miller, L.J.4
  • 31
    • 34247214479 scopus 로고    scopus 로고
    • Role of lysine187 within the second extracellular loop of the type A cholecystokinin receptor in agonist-induced activation. Use of complementary charge-reversal mutagenesis to define a functionally important interdomain interaction
    • Dong, M., Ding, X. Q., Thomas, S. E., Gao, F., Lam, P. C., Abagyan, R., and Miller, L. J. (2007) Role of lysine187 within the second extracellular loop of the type A cholecystokinin receptor in agonist-induced activation. Use of complementary charge-reversal mutagenesis to define a functionally important interdomain interaction. Biochemistry 46, 4522-4531.
    • (2007) Biochemistry , vol.46 , pp. 4522-4531
    • Dong, M.1    Ding, X.Q.2    Thomas, S.E.3    Gao, F.4    Lam, P.C.5    Abagyan, R.6    Miller, L.J.7
  • 32
    • 0000243829 scopus 로고
    • Procheck: A Program to Check the Stereochemical Quality of Protein Structures
    • Laskowski, R. A., Macarthur, M. W., Moss, D. S., and Thornton, J. M. (1993) Procheck: A Program to Check the Stereochemical 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    Moss, D.S.3    Thornton, J.M.4
  • 33
    • 0030047142 scopus 로고    scopus 로고
    • Errors in protein structures [3]
    • Hooft, R. W. W., Vriend, G., Sander, C., and Abola, E. E. (1996) Errors in protein structures. Nature 381, 272-1272 (Pubitemid 26000124)
    • (1996) Nature , vol.381 , Issue.6580 , pp. 272
    • Hooft, R.W.W.1    Vriend, G.2    Sander, C.3    Abola, E.E.4
  • 34
    • 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
  • 35
    • 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
  • 36
    • 0002572979 scopus 로고
    • Cholecystokinin
    • (Walsh, J. H., and Dockray, G. J., Eds.) Raven Press, New York
    • Liddle, R. A. (1994) Cholecystokinin. In Gut Peptides: Biochemistry and Physiology (Walsh, J. H., and Dockray, G. J., Eds.) pp 175-216, Raven Press, New York.
    • (1994) Gut Peptides: Biochemistry and Physiology , pp. 175-216
    • Liddle, R.A.1
  • 37
    • 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


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